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4i98

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Revision as of 19:02, 25 December 2014

Crystal structure of the complex between ScpA(residues 1-160)-ScpB(residues 1-183)

Structural highlights

4i98 is a 3 chain structure with sequence from Strzp. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	4i99
Gene:	scpA, SPP_1876 (STRZP), scpB, SPP_1875 (STRZP)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[SCPA_STRZP] Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpB that pull DNA away from mid-cell into both cell halves (By similarity). [SCPB_STRZP] Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpA that pull DNA away from mid-cell into both cell halves (By similarity).

Publication Abstract from PubMed

Eukaryotic structural maintenance of chromosomes (SMC)-kleisin complexes form large, ring-shaped assemblies that promote accurate chromosome segregation. Their asymmetric structural core comprises SMC heterodimers that associate with both ends of a kleisin subunit. However, prokaryotic condensin Smc-ScpAB is composed of symmetric Smc homodimers associated with the kleisin ScpA in a postulated symmetrical manner. Here, we demonstrate that Smc molecules have two distinct binding sites for ScpA. The N terminus of ScpA binds the Smc coiled coil, whereas the C terminus binds the Smc ATPase domain. We show that in Bacillus subtilis cells, an Smc dimer is bridged by a single ScpAB to generate asymmetric tripartite rings analogous to eukaryotic SMC complexes. We define a molecular mechanism that ensures asymmetric assembly, and we conclude that the basic architecture of SMC-kleisin rings evolved before the emergence of eukaryotes.

An asymmetric SMC-kleisin bridge in prokaryotic condensin.,Burmann F, Shin HC, Basquin J, Soh YM, Gimenez-Oya V, Kim YG, Oh BH, Gruber S Nat Struct Mol Biol. 2013 Jan 27;20(3):371-9. doi: 10.1038/nsmb.2488. Epub 2013, Jan 27. PMID:23353789^[1]

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

References

↑ Burmann F, Shin HC, Basquin J, Soh YM, Gimenez-Oya V, Kim YG, Oh BH, Gruber S. An asymmetric SMC-kleisin bridge in prokaryotic condensin. Nat Struct Mol Biol. 2013 Jan 27;20(3):371-9. doi: 10.1038/nsmb.2488. Epub 2013, Jan 27. PMID:23353789 doi:http://dx.doi.org/10.1038/nsmb.2488

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4i98"

@@ Line 8: / Line 8: @@
 <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=4i98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i98 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4i98 RCSB], [http://www.ebi.ac.uk/pdbsum/4i98 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/SCPA_STRZP SCPA_STRZP]] Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpB that pull DNA away from mid-cell into both cell halves (By similarity). [[http://www.uniprot.org/uniprot/SCPB_STRZP SCPB_STRZP]] Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpA that pull DNA away from mid-cell into both cell halves (By similarity).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

4i98

From Proteopedia

Revision as of 19:02, 25 December 2014

Crystal structure of the complex between ScpA(residues 1-160)-ScpB(residues 1-183)

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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