NMR paper Construction and Crystal Structure Analysis of Heme Acquisition Protein HasA Containing Iron(III)-5,15-Diphenylporphyrin and Derivatives Thereof as an Artificial Prosthetic Group

		BioNMR > Educational resources > Journal club
[NMR paper] Construction and Crystal Structure Analysis of Heme Acquisition Protein HasA Containing Iron(III)-5,15-Diphenylporphyrin and Derivatives Thereof as an Artificial Prosthetic Group

Webservers

NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

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:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

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:

Isotope labeling:

Solid-state NMR:

Thread Tools

Search this Thread

Rate Thread

Display Modes

09-16-2017, 09:58 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,732

Points: 193,617, Level: 100

Level up: 0%, 0 Points needed

Activity: 50.7%

Last Achievements

Award-Showcase

NMR Credits: 0

NMR Points: 193,617

Downloads: 0

Uploads: 0

Construction and Crystal Structure Analysis of Heme Acquisition Protein HasA Containing Iron(III)-5,15-Diphenylporphyrin and Derivatives Thereof as an Artificial Prosthetic Group

Construction and Crystal Structure Analysis of Heme Acquisition Protein HasA Containing Iron(III)-5,15-Diphenylporphyrin and Derivatives Thereof as an Artificial Prosthetic Group

Iron(III)-5,15-diphenylporphyrin (1) and its derivatives (2-7) were accommodated by the heme acquisition protein HasA secreted by Pseudomonas aeruginosa, despite possessing bulky substituents at the meso-position of the porphyrin. Crystal structure analysis revealed that the two phenyl groups at the meso-positions of porphyrin extend outside HasA. It was shown that growth of P. aeruginosa was inhibited in the presence of HasA coordinating the synthetic porphyrins under iron-limiting conditions, and that the structure of the synthetic porphyrins greatly affects the inhibition efficiency.

More...

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
The Iron Chaperone Protein CyaY from Vibriocholerae Is a Heme-Binding Protein The Iron Chaperone Protein CyaY from Vibriocholerae Is a Heme-Binding Protein http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b01304/20170428/images/medium/bi-2016-01304c_0009.gif Biochemistry DOI: 10.1021/acs.biochem.6b01304 http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/bichaw/~4/uWkt60WW2AI More...	nmrlearner	Journal club	0	04-29-2017 04:33 AM
Cytoplasmic Heme-Binding Protein (HutX) from Vibrio cholerae Is an Intracellular Heme Transport Proteinfor the Heme-Degrading Enzyme, HutZ Cytoplasmic Heme-Binding Protein (HutX) from Vibrio cholerae Is an Intracellular Heme Transport Proteinfor the Heme-Degrading Enzyme, HutZ http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b01273/20160203/images/medium/bi-2015-01273d_0009.gif Biochemistry DOI: 10.1021/acs.biochem.5b01273 http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/bichaw/~4/TZY3CBAo0xw More...	nmrlearner	Journal club	0	02-04-2016 11:46 AM
[NMR paper] Artificial heme-proteins: determination of axial ligand orientations through paramagnetic NMR shifts. Artificial heme-proteins: determination of axial ligand orientations through paramagnetic NMR shifts. Related Articles Artificial heme-proteins: determination of axial ligand orientations through paramagnetic NMR shifts. Chem Commun (Camb). 2014 Mar 3; Authors: Vicari C, Saraiva IH, Maglio O, Nastri F, Pavone V, Louro RO, Lombardi A Abstract An empirical equation, describing the relationship between the porphyrin methyl hyperfine shifts and the position of the axial ligand(s), has been applied to an artificial heme-protein in order to...	nmrlearner	Journal club	0	03-04-2014 06:37 PM
Dynamics of heme in hemoproteins: proton NMR study of myoglobin reconstituted with iron 3-ethyl-2-methylporphyrin. Dynamics of heme in hemoproteins: proton NMR study of myoglobin reconstituted with iron 3-ethyl-2-methylporphyrin. Dynamics of heme in hemoproteins: proton NMR study of myoglobin reconstituted with iron 3-ethyl-2-methylporphyrin. Biochim Biophys Acta. 2011 May 6; Authors: Juillard S, Chevance S, Bondon A, Simonneaux G The asymmetric 3-ethyl-2-methylporphyrin iron complex was synthetized and inserted into apomyoglobin. UV-visible spectroscopic studies demonstrated the capacity of iron to coordinate different exogenous axial ligands in ferrous and...	nmrlearner	Journal club	0	05-24-2011 12:00 PM
[NMR paper] Automated analysis of protein NMR assignments using methods from artificial intellige Automated analysis of protein NMR assignments using methods from artificial intelligence. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Automated analysis of protein NMR assignments using methods from artificial intelligence. J Mol Biol. 1997 Jun 20;269(4):592-610 Authors: Zimmerman DE, Kulikowski CA, Huang Y, Feng W, Tashiro M, Shimotakahara S, Chien C, Powers R, Montelione GT An expert system for determining resonance assignments from NMR spectra of proteins is...	nmrlearner	Journal club	0	08-22-2010 03:31 PM
[NMR paper] Automated analysis of protein NMR assignments using methods from artificial intellige Automated analysis of protein NMR assignments using methods from artificial intelligence. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Automated analysis of protein NMR assignments using methods from artificial intelligence. J Mol Biol. 1997 Jun 20;269(4):592-610 Authors: Zimmerman DE, Kulikowski CA, Huang Y, Feng W, Tashiro M, Shimotakahara S, Chien C, Powers R, Montelione GT An expert system for determining resonance assignments from NMR spectra of proteins is...	nmrlearner	Journal club	0	08-22-2010 03:03 PM
[NMR paper] Bis-methionine ligation to heme iron in mutants of cytochrome b562. 2. Characterizati Bis-methionine ligation to heme iron in mutants of cytochrome b562. 2. Characterization by NMR of heme-ligand interactions. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Bis-methionine ligation to heme iron in mutants of cytochrome b562. 2. Characterization by NMR of heme-ligand interactions. Biochemistry. 1996 Oct 22;35(42):13627-35 Authors: Barker PD, Freund SM Previous work has shown that, in variants of cytochrome b562 containing the H102M mutation, methionine residues provide both...	nmrlearner	Journal club	0	08-22-2010 02:20 PM
[NMR paper] 1H NMR study of the influence of hydrophobic contacts on protein-prosthetic group rec 1H NMR study of the influence of hydrophobic contacts on protein-prosthetic group recognition in bovine and rat ferricytochrome b5. Related Articles 1H NMR study of the influence of hydrophobic contacts on protein-prosthetic group recognition in bovine and rat ferricytochrome b5. Biochemistry. 1990 Oct 16;29(41):9623-31 Authors: Lee KB, La Mar GN, Kehres LA, Fujinari EM, Smith KM, Pochapsky TC, Sligar SG The proton nuclear magnetic resonance spectra of the soluble fragment of native bovine and genetically engineered wild-type rat...	nmrlearner	Journal club	0	08-21-2010 11:04 PM

« Previous Thread | Next Thread »

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