1hf2

From Proteopedia

(Difference between revisions)

Revision as of 10:31, 18 November 2020

Crystal structure of the bacterial cell-division inhibitor MinC from T. maritima

Structural highlights

1hf2 is a 4 chain structure with sequence from Atcc 43589. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	MINC (ATCC 43589)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MINC_THEMA] Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Bacterial cell division requires accurate selection of the middle of the cell, where the bacterial tubulin homologue FtsZ polymerizes into a ring structure. In Escherichia coli, site selection is dependent on MinC, MinD and MINE: MinC acts, with MinD, to inhibit division at sites other than the midcell by directly interacting with FTSZ: Here we report the crystal structure to 2.2 A of MinC from Thermotoga maritima. MinC consists of two domains separated by a short linker. The C-terminal domain is a right-handed beta-helix and is involved in dimer formation. The crystals contain two different MinC dimers, demonstrating flexibility in the linker region. The two-domain architecture and dimerization of MinC can be rationalized with a model of cell division inhibition. MinC does not act like SulA, which affects the GTPase activity of FtsZ, and the model can explain how MinC would select for the FtsZ polymer rather than the monomer.

Crystal structure of the bacterial cell division inhibitor MinC.,Cordell SC, Anderson RE, Lowe J EMBO J. 2001 May 15;20(10):2454-61. PMID:11350934^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Cordell SC, Anderson RE, Lowe J. Crystal structure of the bacterial cell division inhibitor MinC. EMBO J. 2001 May 15;20(10):2454-61. PMID:11350934 doi:10.1093/emboj/20.10.2454

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hf2"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the bacterial cell-division inhibitor MinC from T. maritima==
-<StructureSection load='1hf2' size='340' side='right' caption='[[1hf2]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+<StructureSection load='1hf2' size='340' side='right'caption='[[1hf2]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1hf2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HF2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HF2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1hf2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HF2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1HF2 FirstGlance]. <br>
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MINC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</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=1hf2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hf2 OCA], [http://pdbe.org/1hf2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hf2 RCSB], [http://www.ebi.ac.uk/pdbsum/1hf2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hf2 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1hf2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hf2 OCA], [http://pdbe.org/1hf2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hf2 RCSB], [http://www.ebi.ac.uk/pdbsum/1hf2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hf2 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 33: / Line 33: @@
 </StructureSection>
 [[Category: Atcc 43589]]
+[[Category: Large Structures]]
 [[Category: Anderson, R E]]
 [[Category: Cordell, S C]]

1hf2

From Proteopedia

Revision as of 10:31, 18 November 2020

Crystal structure of the bacterial cell-division inhibitor MinC from T. maritima

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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