|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of a bacterial cell-surface flagellin== | | ==Crystal structure of a bacterial cell-surface flagellin== |
| - | <StructureSection load='2zbi' size='340' side='right' caption='[[2zbi]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='2zbi' size='340' side='right'caption='[[2zbi]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2zbi]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Sphingomonas_sp._a1 Sphingomonas sp. a1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZBI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZBI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2zbi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingomonas_sp._a1 Sphingomonas sp. a1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZBI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZBI FirstGlance]. <br> |
| | </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> | | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FliC ([https://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://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> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2zbi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zbi OCA], [https://pdbe.org/2zbi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zbi RCSB], [https://www.ebi.ac.uk/pdbsum/2zbi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zbi ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| Line 29: |
Line 29: |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Flagella%2C bacterial|Flagella%2C bacterial]] | + | *[[Flagellin 3D structures|Flagellin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Sphingomonas sp. a1]] | | [[Category: Sphingomonas sp. a1]] |
| | [[Category: Maruyama, Y]] | | [[Category: Maruyama, Y]] |
| Structural highlights
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.
See Also
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
|
