1hyq
From Proteopedia
(New page: 200px<br /><applet load="1hyq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hyq, resolution 2.6Å" /> '''MIND BACTERIAL CELL D...) |
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| - | [[Image:1hyq.jpg|left|200px]]<br /><applet load="1hyq" size=" | + | [[Image:1hyq.jpg|left|200px]]<br /><applet load="1hyq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hyq, resolution 2.6Å" /> | caption="1hyq, resolution 2.6Å" /> | ||
'''MIND BACTERIAL CELL DIVISION REGULATOR FROM A. FULGIDUS'''<br /> | '''MIND BACTERIAL CELL DIVISION REGULATOR FROM A. FULGIDUS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | In bacterial cell division MinD plays a pivotal role, selecting the | + | 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== | ==About this Structure== | ||
| - | 1HYQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http:// | + | 1HYQ is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: Archaeoglobus fulgidus]] | [[Category: Archaeoglobus fulgidus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cordell, S | + | [[Category: Cordell, S C.]] |
[[Category: Lowe, J.]] | [[Category: Lowe, J.]] | ||
[[Category: bacterial cell division]] | [[Category: bacterial cell division]] | ||
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[[Category: minc]] | [[Category: minc]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:06:11 2008'' |
Revision as of 11:06, 21 February 2008
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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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