1e4g: Difference between revisions
New page: left|200px<br /><applet load="1e4g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e4g, resolution 2.6Å" /> '''FTSA (ATP-BOUND FORM)... |
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[[Image:1e4g.jpg|left|200px]]<br /><applet load="1e4g" size=" | [[Image:1e4g.jpg|left|200px]]<br /><applet load="1e4g" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1e4g, resolution 2.6Å" /> | caption="1e4g, resolution 2.6Å" /> | ||
'''FTSA (ATP-BOUND FORM) FROM THERMOTOGA MARITIMA'''<br /> | '''FTSA (ATP-BOUND FORM) FROM THERMOTOGA MARITIMA'''<br /> | ||
==Overview== | ==Overview== | ||
Bacterial cell division requires formation of a septal ring. A key step in | Bacterial cell division requires formation of a septal ring. A key step in septum formation is polymerization of FtsZ. FtsA directly interacts with FtsZ and probably targets other proteins to the septum. We have solved the crystal structure of FtsA from Thermotoga maritima in the apo and ATP-bound form. FtsA consists of two domains with the nucleotide-binding site in the interdomain cleft. Both domains have a common core that is also found in the actin family of proteins. Structurally, FtsA is most homologous to actin and heat-shock cognate protein (Hsc70). An important difference between FtsA and the actin family of proteins is the insertion of a subdomain in FtsA. Movement of this subdomain partially encloses a groove, which could bind the C-terminus of FtsZ. FtsZ is the bacterial homologue of tubulin, and the FtsZ ring is functionally similar to the contractile ring in dividing eukaryotic cells. Elucidation of the crystal structure of FtsA shows that another bacterial protein involved in cytokinesis is structurally related to a eukaryotic cytoskeletal protein involved in cytokinesis. | ||
==About this Structure== | ==About this Structure== | ||
1E4G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with MG and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1E4G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E4G OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
[[Category: Ent, F | [[Category: Ent, F Van Den.]] | ||
[[Category: Lowe, J.]] | [[Category: Lowe, J.]] | ||
[[Category: ATP]] | [[Category: ATP]] | ||
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[[Category: bacterial cell division]] | [[Category: bacterial cell division]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:23:42 2008'' | ||
Revision as of 13:23, 21 February 2008
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FTSA (ATP-BOUND FORM) FROM THERMOTOGA MARITIMA
OverviewOverview
Bacterial cell division requires formation of a septal ring. A key step in septum formation is polymerization of FtsZ. FtsA directly interacts with FtsZ and probably targets other proteins to the septum. We have solved the crystal structure of FtsA from Thermotoga maritima in the apo and ATP-bound form. FtsA consists of two domains with the nucleotide-binding site in the interdomain cleft. Both domains have a common core that is also found in the actin family of proteins. Structurally, FtsA is most homologous to actin and heat-shock cognate protein (Hsc70). An important difference between FtsA and the actin family of proteins is the insertion of a subdomain in FtsA. Movement of this subdomain partially encloses a groove, which could bind the C-terminus of FtsZ. FtsZ is the bacterial homologue of tubulin, and the FtsZ ring is functionally similar to the contractile ring in dividing eukaryotic cells. Elucidation of the crystal structure of FtsA shows that another bacterial protein involved in cytokinesis is structurally related to a eukaryotic cytoskeletal protein involved in cytokinesis.
About this StructureAbout this Structure
1E4G is a Single protein structure of sequence from Thermotoga maritima with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the cell division protein FtsA from Thermotoga maritima., van den Ent F, Lowe J, EMBO J. 2000 Oct 16;19(20):5300-7. PMID:11032797
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