5e1l
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Structural and functional analysis of the E. coli FtsZ interacting protein, ZapC, reveals insight into molecular properties of a novel Z ring stabilizing protein== |
| - | + | <StructureSection load='5e1l' size='340' side='right' caption='[[5e1l]], [[Resolution|resolution]] 2.15Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5e1l]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E1L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E1L FirstGlance]. <br> | |
| - | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5e1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e1l OCA], [http://pdbe.org/5e1l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e1l RCSB], [http://www.ebi.ac.uk/pdbsum/5e1l PDBsum]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | [[ | + | [[http://www.uniprot.org/uniprot/W8SPQ2_ECOLX W8SPQ2_ECOLX]] Contributes to the efficiency of the cell division process by stabilizing the polymeric form of the cell division protein FtsZ. Acts by promoting interactions between FtsZ protofilaments and suppressing the GTPase activity of FtsZ.[HAMAP-Rule:MF_00906][PIRNR:PIRNR010252] |
| - | [[Category: | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Huang, K H]] | ||
[[Category: Janakiraman, A]] | [[Category: Janakiraman, A]] | ||
| + | [[Category: Schumacher, M A]] | ||
| + | [[Category: Tchorzewski, L]] | ||
[[Category: Zeng, W]] | [[Category: Zeng, W]] | ||
| - | [[Category: | + | [[Category: Cell cycle]] |
| - | [[Category: | + | [[Category: Cell division]] |
| + | [[Category: Z ring]] | ||
Revision as of 12:48, 23 December 2015
Structural and functional analysis of the E. coli FtsZ interacting protein, ZapC, reveals insight into molecular properties of a novel Z ring stabilizing protein
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