1hyq
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1hyq.jpg|left|200px]] | + | [[Image:1hyq.jpg|left|200px]] |
| - | + | ||
| - | '''MIND BACTERIAL CELL DIVISION REGULATOR FROM A. FULGIDUS''' | + | {{Structure |
| + | |PDB= 1hyq |SIZE=350|CAPTION= <scene name='initialview01'>1hyq</scene>, resolution 2.6Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= AF0696 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2234 Archaeoglobus fulgidus]) | ||
| + | }} | ||
| + | |||
| + | '''MIND BACTERIAL CELL DIVISION REGULATOR FROM A. FULGIDUS''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1HYQ is a [ | + | 1HYQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HYQ OCA]. |
==Reference== | ==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:[http:// | + | Crystal structure of the bacterial cell division regulator MinD., Cordell SC, Lowe J, FEBS Lett. 2001 Mar 9;492(1-2):160-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11248256 11248256] |
[[Category: Archaeoglobus fulgidus]] | [[Category: Archaeoglobus fulgidus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 19: | Line 28: | ||
[[Category: minc]] | [[Category: minc]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:43:24 2008'' |
Revision as of 09:43, 20 March 2008
| |||||||
| , resolution 2.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | AF0696 (Archaeoglobus fulgidus) | ||||||
| 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
Page seeded by OCA on Thu Mar 20 11:43:24 2008
