1hyq

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|ACTIVITY=
|ACTIVITY=
|GENE= AF0696 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2234 Archaeoglobus fulgidus])
|GENE= AF0696 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2234 Archaeoglobus fulgidus])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hyq OCA], [http://www.ebi.ac.uk/pdbsum/1hyq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hyq RCSB]</span>
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[[Category: minc]]
[[Category: minc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:12:10 2008''

Revision as of 18:12, 30 March 2008


PDB ID 1hyq

Drag the structure with the mouse to rotate
, resolution 2.6Å
Gene: AF0696 (Archaeoglobus fulgidus)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

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