Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.

		BioNMR > Educational resources > Journal club
Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.

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

12-15-2010, 12:03 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,779

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

Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.

Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.

Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.

J Struct Funct Genomics. 2010 Dec 14;

Authors: Mani R, Vorobiev S, Swapna GV, Neely H, Janjua H, Ciccosanti C, Xiao R, Acton TB, Everett JK, Hunt J, Montelione GT

The conserved Lipoprotein-17 domain of membrane-associated protein Q9PRA0_UREPA from Ureaplasma parvum was selected for structure determination by the Northeast Structural Genomics Consortium, as part of the Protein Structure Initiative's program on structure-function analysis of protein domains from large domain sequence families lacking structural representatives. The 100-residue Lipoprotein-17 domain is a "domain of unknown function" (DUF) that is a member of Pfam protein family PF04200, a large domain family for which no members have characterized biochemical functions. The three-dimensional structure of the Lipoprotein-17 domain of protein Q9PRA0_UREPA was determined by both solution NMR and by X-ray crystallography at 2.5*Å. The two structures are in good agreement with each other. The domain structure features three ?-helices, ?1 through ?3, and five ?-strands. Strands ?1/?2, ?3/?4, ?4/?5 are anti-parallel to each other. Strands ?1and ?2 are orthogonal to strands ?3, ?4, ?5, while helix ?3 is formed between the strands ?3 and ?4. One-turn helix ?2 is formed between the strands ?1 and ?2, while helix ?1 occurs in the N-terminal polypeptide segment. Searches of the Protein Data Bank do not identify any other protein with significant structural similarity to Lipoprotein-17 domain of Q9PRA0_UREPA, indicating that it is a novel protein fold.

PMID: 21153711 [PubMed - as supplied by publisher]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Spectroscopic solution: NMR accesses membrane protein structures Spectroscopic solution: NMR accesses membrane protein structures Membrane proteins mediate so much of the information flow between cells and their surroundings. Understanding their molecular structure will inevitably give scientists insights into function and form as well as providing targets for novel pharmaceuticals when these proteins go awry. Source: Spectroscopynow.com	nmrlearner	General	0	10-03-2011 08:40 PM
[NMR paper] NMR structural studies reveal a novel protein fold for MerB, the organomercurial lyas NMR structural studies reveal a novel protein fold for MerB, the organomercurial lyase involved in the bacterial mercury resistance system. Related Articles NMR structural studies reveal a novel protein fold for MerB, the organomercurial lyase involved in the bacterial mercury resistance system. Biochemistry. 2004 Jul 6;43(26):8322-32 Authors: Di Lello P, Benison GC, Valafar H, Pitts KE, Summers AO, Legault P, Omichinski JG Mercury resistant bacteria have developed a system of two enzymes (MerA and MerB), which allows them to efficiently...	nmrlearner	Journal club	0	11-24-2010 09:51 PM
[NMR paper] Fatty acid interactions with proteins: what X-ray crystal and NMR solution structures Fatty acid interactions with proteins: what X-ray crystal and NMR solution structures tell us. Related Articles Fatty acid interactions with proteins: what X-ray crystal and NMR solution structures tell us. Prog Lipid Res. 2004 May;43(3):177-99 Authors: Hamilton JA The interactions of fatty acids with proteins have been studied by a variety of conventional approaches for decades. However, only limited aspects of fatty acid-protein interactions have been elucidated, even with the integration of information gleaned from the many techniques....	nmrlearner	Journal club	0	11-24-2010 09:51 PM
[NMR paper] Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interact Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapD. Related Articles Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapD. Proc Natl Acad Sci U S A. 2002 Jan 22;99(2):709-14 Authors: Bann JG, Pinkner J, Hultgren SJ, Frieden C PapD is a periplasmic chaperone essential for P pilus formation in pyelonephritic strains of E. coli. It is composed of two domains, each of which contains a tryptophan...	nmrlearner	Journal club	0	11-24-2010 08:49 PM
[NMR paper] NMR solution structure of complement-like repeat CR3 from the low density lipoprotein NMR solution structure of complement-like repeat CR3 from the low density lipoprotein receptor-related protein. Evidence for specific binding to the receptor binding domain of human alpha(2)-macroglobulin. Related Articles NMR solution structure of complement-like repeat CR3 from the low density lipoprotein receptor-related protein. Evidence for specific binding to the receptor binding domain of human alpha(2)-macroglobulin. J Biol Chem. 2000 Feb 4;275(5):3264-9 Authors: Dolmer K, Huang W, Gettins PG We have used NMR methods to determine the...	nmrlearner	Journal club	0	11-18-2010 09:15 PM
[NMR paper] Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal prote Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR. Related Articles Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR. Biochemistry. 1994 Apr 19;33(15):4721-9 Authors: Gallagher T, Alexander P, Bryan P, Gilliland GL The structure of the 56-residue B1 immunoglobulin-binding domain from streptococcal protein G has been determined in two different crystal forms. The crystal structures were deduced by molecular...	nmrlearner	Journal club	0	08-22-2010 03:33 AM
[NMR paper] Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal prote Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR. Related Articles Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR. Biochemistry. 1994 Apr 19;33(15):4721-9 Authors: Gallagher T, Alexander P, Bryan P, Gilliland GL The structure of the 56-residue B1 immunoglobulin-binding domain from streptococcal protein G has been determined in two different crystal forms. The crystal structures were deduced by molecular...	nmrlearner	Journal club	0	08-22-2010 03:33 AM
[NMR paper] NMR solution structure of complement-like repeat CR8 from the low density lipoprotein NMR solution structure of complement-like repeat CR8 from the low density lipoprotein receptor-related protein. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles NMR solution structure of complement-like repeat CR8 from the low density lipoprotein receptor-related protein. J Biol Chem. 1999 May 14;274(20):14130-6 Authors: Huang W, Dolmer K, Gettins PG The low density lipoprotein receptor-related protein is a member of the low density...	nmrlearner	Journal club	0	08-21-2010 04:03 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