1hyq

From Proteopedia

Revision as of 11:06, 21 February 2008 by OCA (Talk | contribs)
Jump to: navigation, search
Image:1hyq.jpg

1hyq, resolution 2.6Å

Drag the structure with the mouse to rotate

MIND BACTERIAL CELL DIVISION REGULATOR FROM A. FULGIDUS

Overview

In bacterial cell division MinD plays a pivotal role, selecting the mid-cell over other sites. With MinC, MinD forms a non-specific inhibitor of division, that interacts with FtsZ. Specificity is provided by MinD's interaction with MinE at the mid-cell. We have solved the crystal structure of MinD-1 from Archaeoglobus fulgidus to 2.6 A by multiple anomalous dispersion. MinD is a classic nucleotide binding protein, related to nitrogenase iron proteins, which have a fold of a seven-stranded parallel beta-sheet, surrounded by alpha-helices. Although MinD, unlike the proteins it interacts with and those it is structurally related to, is a monomer, not a dimer.

About this Structure

1HYQ is a Single protein structure of sequence from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.

Reference

Crystal structure of the bacterial cell division regulator MinD., Cordell SC, Lowe J, FEBS Lett. 2001 Mar 9;492(1-2):160-5. PMID:11248256

Page seeded by OCA on Thu Feb 21 13:06:11 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hyq"
Personal tools