2zbi

From Proteopedia

(Difference between revisions)

Revision as of 07:57, 11 August 2016

Crysatl structure of a bacterial cell-surface flagellin

Structural highlights

2zbi is a 2 chain structure with sequence from Sphingomonas sp. a1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Gene:	FliC (Sphingomonas sp. A1)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Bacterial flagellins are generally self-assembled into extracellular flagella for cell motility. However, the flagellin homologue p5 is found on the cell surface of Sphingomonas sp. A1 (strain A1) and binds tightly to the alginate polysaccharide. To assimilate alginate, strain A1 forms a mouthlike pit on the cell surface and concentrates the polymer in the pit. p5 is a candidate receptor that recognizes extracellular alginate and controls pit formation. To improve our understanding of the structure and function of p5, we determined the crystal structure of truncated p5 (p5DeltaN53C45) at 2.0 A resolution. This, to our knowledge, is the first structure of flagellin_IN motif-containing flagellin. p5DeltaN53C45 consists of two domains: an alpha-domain rich in alpha-helices that forms the N- and C-terminal regions and a beta-domain rich in beta-strands that constitutes the central region. The alpha-domain is structurally similar to the D1 domain of Salmonella typhimurium flagellin, while the beta-domain is structurally similar to the finger domain of the bacteriophage T4 baseplate protein that is important for intermolecular interactions between baseplate and a long or short tail fiber. Results from the deletion mutant analysis suggest that residues 20-40 and 353-363 are responsible for alginate binding. Truncated N- and C-terminal regions are thought to constitute alpha-helices extending from the alpha-domain. On the basis of the size and surface charge, the cleft in extended alpha-helices is proposed as an alginate binding site of p5. Structural similarity in the beta-domain suggests that the beta-domain is involved in the proper localization and/or orientation of p5 on the cell surface.

Crystal structure of a novel bacterial cell-surface flagellin binding to a polysaccharide(,).,Maruyama Y, Momma M, Mikami B, Hashimoto W, Murata K Biochemistry. 2008 Feb 5;47(5):1393-402. Epub 2008 Jan 12. PMID:18189419^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Maruyama Y, Momma M, Mikami B, Hashimoto W, Murata K. Crystal structure of a novel bacterial cell-surface flagellin binding to a polysaccharide(,). Biochemistry. 2008 Feb 5;47(5):1393-402. Epub 2008 Jan 12. PMID:18189419 doi:10.1021/bi701872x

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2zbi"

Categories: Sphingomonas sp. a1 | Maruyama, Y | Flagellin | Flagellum | Structural protein

@@ Line 1: / Line 1: @@
 ==Crysatl structure of a bacterial cell-surface flagellin==
 <StructureSection load='2zbi' size='340' side='right' caption='[[2zbi]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FliC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90322 Sphingomonas sp. A1])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zbi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zbi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zbi RCSB], [http://www.ebi.ac.uk/pdbsum/2zbi PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zbi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zbi OCA], [http://pdbe.org/2zbi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zbi RCSB], [http://www.ebi.ac.uk/pdbsum/2zbi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zbi ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 15: / Line 16: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2zbi ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 25: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2zbi" style="background-color:#fffaf0;"></div>
 ==See Also==

2zbi

From Proteopedia

Revision as of 07:57, 11 August 2016

Crysatl structure of a bacterial cell-surface flagellin

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox