BioNMR
NMR aggregator & online community since 2003
BioNMR    
Learn or help to learn NMR - get free NMR books!
 

Go Back   BioNMR > Educational resources > Journal club
Advanced Search
Home Forums Wiki NMR feeds Downloads Register Today's Posts



Jobs Groups Conferences Literature Pulse sequences Software forums Programs Sample preps Web resources BioNMR issues


Webservers
NMR processing:
MDD
NMR assignment:
Backbone:
Autoassign
MARS
UNIO Match
PINE
Side-chains:
UNIO ATNOS-Ascan
NOEs:
UNIO ATNOS-Candid
UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
UNIO Candid
Fragment-based:
BMRB CS-Rosetta
Rosetta-NMR (Robetta)
Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
Simshift
Torsion angles from chemical shifts:
Preditor
TALOS
Promega- Proline
Secondary structure from chemical shifts:
CSI (via RCI server)
TALOS
MICS caps, β-turns
d2D
PECAN
Flexibility from chemical shifts:
RCI
Interactions from chemical shifts:
HADDOCK
Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
NOEs, other restraints:
PROSESS
PSVS
RPF scores
iCing
Chemical shifts:
PROSESS
CheShift2
Vasco
iCing
RDCs:
DC
Anisofit
Pseudocontact shifts:
Anisofit
Protein geomtery:
Resolution-by-Proxy
PROSESS
What-If
iCing
PSVS
MolProbity
SAVES2 or SAVES4
Vadar
Prosa
ProQ
MetaMQAPII
PSQS
Eval123D
STAN
Ramachandran Plot
Rampage
ERRAT
Verify_3D
Harmony
Quality Control Check
NMR spectrum prediction:
FANDAS
MestReS
V-NMR
Flexibility from structure:
Backbone S2
Methyl S2
B-factor
Molecular dynamics:
Gromacs
Amber
Antechamber
Chemical shifts prediction:
From structure:
Shiftx2
Sparta+
Camshift
CH3shift- Methyl
ArShift- Aromatic
ShiftS
Proshift
PPM
CheShift-2- Cα
From sequence:
Shifty
Camcoil
Poulsen_rc_CS
Disordered proteins:
MAXOCC
Format conversion & validation:
CCPN
From NMR-STAR 3.1
Validate NMR-STAR 3.1
NMR sample preparation:
Protein disorder:
DisMeta
Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


Reply
 
Thread Tools Search this Thread Rate Thread Display Modes
  #1  
Old 01-28-2015, 03:22 AM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,732
Points: 193,617, Level: 100
Points: 193,617, Level: 100 Points: 193,617, Level: 100 Points: 193,617, Level: 100
Level up: 0%, 0 Points needed
Level up: 0% Level up: 0% Level up: 0%
Activity: 50.7%
Activity: 50.7% Activity: 50.7% Activity: 50.7%
Last Achievements
Award-Showcase
NMR Credits: 0
NMR Points: 193,617
Downloads: 0
Uploads: 0
Default An NMR method to probe molecular influences of substrate loading in NRPS carrier proteins.

An NMR method to probe molecular influences of substrate loading in NRPS carrier proteins.

Related Articles An NMR method to probe molecular influences of substrate loading in NRPS carrier proteins.

Biochemistry. 2015 Jan 26;

Authors: Goodrich AC, Frueh DP

Abstract
Carrier proteins (CPs) play a central role in nonribosomal peptide (NRP) synthesis by shuttling covalently attached substrates between active sites. Understanding how the covalent attachment of a substrate (loading) influences the molecular properties of CPs is key to determining the mechanism of NRP synthesis. However, structural studies have been impaired by substrate hydrolysis. Here, we used nuclear magnetic resonance spectroscopy to monitor substrate loading of a CP and to overcome hydrolysis. Our results reveal the spectroscopic signature of substrate loading and provide evidence of molecular communication between an NRPS carrier protein and its covalently attached substrate.


PMID: 25620398 [PubMed - as supplied by publisher]



More...
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
Influence of Substrate Modification and C-Terminal Truncation on the Active Site Structure of Substrate-Bound Heme Oxygenase from Neisseriae meningitidis. A 1H NMR Study
Influence of Substrate Modification and C-Terminal Truncation on the Active Site Structure of Substrate-Bound Heme Oxygenase from Neisseriae meningitidis. A 1H NMR Study http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi200978g/aop/images/medium/bi-2011-00978g_0009.gif Biochemistry DOI: 10.1021/bi200978g http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/bichaw/~4/BYT7Ijd6pDI More...
nmrlearner Journal club 0 09-22-2011 05:37 AM
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study.
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study. Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study. Biochemistry. 2011 Aug 27; Authors: Peng D, Satterlee JD, Ma LH, Dallas JL, Smith KM, Zhang X, Sato M, La Mar GN Abstract Heme oxygenase, HO, from the pathogenic bacterium N. meningitidis, NmHO, which...
nmrlearner Journal club 0 08-30-2011 04:52 PM
[Question from NMRWiki Q&A forum] Tuning probe failed after a dual probe was replaced with a BBI probe
Tuning probe failed after a dual probe was replaced with a BBI probe We generally use Dual to run 13C and BBI to run 2D. After changed the probe, the command "edhead" was used to set the probe. Put the sample tube, lock the solvent, and then type "atma" to tune the probe. We always do it like this, but now we can not tune the proton after installed the BBI probe (13C is OK). The dip can not be found by "atma", and "atmm" was also not work on forming a dip. What is the most possible reason for this error? How to solve it and avoid it in the future ? Thanks. (Instrument: Bruker 400 MHz,...
nmrlearner News from other NMR forums 0 08-23-2011 05:31 PM
Engineering [Ln(DPA)3]3â?? binding sites in proteins: a widely applicable method for tagging proteins with lanthanide ions
Engineering 3â?? binding sites in proteins: a widely applicable method for tagging proteins with lanthanide ions Abstract Paramagnetic relaxation enhancements from unpaired electrons observed in nuclear magnetic resonance (NMR) spectra present powerful long-range distance restraints. The most frequently used paramagnetic tags, however, are tethered to the protein via disulfide bonds, requiring proteins with single cysteine residues for covalent attachment. Here we present a straightforward strategy to tag proteins site-specifically with paramagnetic lanthanides without a tether and...
nmrlearner Journal club 0 07-26-2011 11:11 AM
[NMR tweet] http://www.book-lib.com/methods-in-molecular-biophysics-structure-dynamics-function.html #nuclear #magnetic #resonance #molecular Method
http://www.book-lib.com/methods-in-molecular-biophysics-structure-dynamics-function.html #nuclear #magnetic #resonance #molecular Method Published by booklib2011 (Books For Your Life) on 2011-04-12T07:02:21Z Source: Twitter
nmrlearner Twitter NMR 0 04-12-2011 07:13 AM
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes. Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes. J Inorg Biochem. 2010 Oct;104(10):1063-70 Authors: Du Z, Unno M, Matsui T, Ikeda-Saito M, La Mar GN Proton 2D NMR was used to confirm in solution a highly conserved portion of the molecular structure upon substrate loss for the...
nmrlearner Journal club 0 02-10-2011 03:51 PM
[NMR paper] Weak substrate binding to transport proteins studied by NMR.
Weak substrate binding to transport proteins studied by NMR. Related Articles Weak substrate binding to transport proteins studied by NMR. Biophys J. 1998 Dec;75(6):2794-800 Authors: Spooner PJ, O'Reilly WJ, Homans SW, Rutherford NG, Henderson PJ, Watts A The weak binding of sugar substrates fails to induce any quantifiable physical changes in the L-fucose-H+ symport protein, FucP, from Escherichia coli, and this protein lacks any strongly binding ligands for competitive binding assays. Access to substrate binding behavior is however possible...
nmrlearner Journal club 0 11-17-2010 11:15 PM
[NMR paper] Chemical shift as a probe of molecular interfaces: NMR studies of DNA binding by the
Chemical shift as a probe of molecular interfaces: NMR studies of DNA binding by the three amino-terminal zinc finger domains from transcription factor IIIA. Related Articles Chemical shift as a probe of molecular interfaces: NMR studies of DNA binding by the three amino-terminal zinc finger domains from transcription factor IIIA. J Biomol NMR. 1998 Jul;12(1):51-71 Authors: Foster MP, Wuttke DS, Clemens KR, Jahnke W, Radhakrishnan I, Tennant L, Reymond M, Chung J, Wright PE We report the NMR resonance assignments for a macromolecular...
nmrlearner Journal club 0 11-17-2010 11:15 PM



Posting Rules
You may not post new threads
You may not post replies
You may not post attachments
You may not edit your posts

BB code is On
Smilies are On
[IMG] code is On
HTML code is On
Trackbacks are Off
Pingbacks are Off
Refbacks are Off



BioNMR advertisements to pay for website hosting and domain registration. Nobody does it for us.



Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2024, Jelsoft Enterprises Ltd.
Copyright, BioNMR.com, 2003-2013
Search Engine Friendly URLs by vBSEO 3.6.0

All times are GMT. The time now is 11:30 AM.


Map