1hyq

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{{STRUCTURE_1hyq| PDB=1hyq | SCENE= }}
{{STRUCTURE_1hyq| PDB=1hyq | SCENE= }}
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'''MIND BACTERIAL CELL DIVISION REGULATOR FROM A. FULGIDUS'''
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===MIND BACTERIAL CELL DIVISION REGULATOR FROM A. FULGIDUS===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11248256 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11248256}}
==About this Structure==
==About this Structure==
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[[Category: Ftsz]]
[[Category: Ftsz]]
[[Category: Minc]]
[[Category: Minc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:08:38 2008''

Revision as of 07:08, 1 July 2008

Image:1hyq.png

Template:STRUCTURE 1hyq

MIND BACTERIAL CELL DIVISION REGULATOR FROM A. FULGIDUS

Template:ABSTRACT PUBMED 11248256

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

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