This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2zbi

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2zbi.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2zbi.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2zbi| PDB=2zbi | SCENE= }}
{{STRUCTURE_2zbi| PDB=2zbi | SCENE= }}
-
'''Crysatl structure of a bacterial cell-surface flagellin'''
+
===Crysatl structure of a bacterial cell-surface flagellin===
-
==Overview==
+
<!--
-
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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18189419}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18189419 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18189419}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Flagellum]]
[[Category: Flagellum]]
[[Category: Structural protein]]
[[Category: Structural protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:07:11 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:21:42 2008''

Revision as of 01:21, 29 July 2008

Image:2zbi.png

Template:STRUCTURE 2zbi

Crysatl structure of a bacterial cell-surface flagellin

Template:ABSTRACT PUBMED 18189419

About this Structure

2ZBI is a Single protein structure of sequence from Sphingomonas sp. a1. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Tue Jul 29 04:21:42 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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