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2m45

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Revision as of 17:29, 9 March 2017

NMR solution structure of the C-terminus of the minichromosome maintenance protein MCM from Sulfolobus solfataricus

Structural highlights

2m45 is a 1 chain structure with sequence from Sulso. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	MCM, SSO0774 (SULSO)
Activity:	DNA helicase, with EC number 3.6.4.12
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MCM_SULSO] Presumptive replicative helicase. Has ATPase and DNA helicase activities. The latter preferentially melts 5'-tailed oligonucleotides and is stimulated by the SSB protein (single-stranded DNA binding protein). The active ATPase sites in the MCM ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The helicase function is proposed to use a partially sequential mode of ATP hydrolysis; the complex appears to tolerate multiple catalytically inactive subunits.^[1]

Publication Abstract from PubMed

The minichromosome maintenance complex (MCM) represents the replicative DNA helicase both in eukaryotes and archaea. Here, we describe the solution structure of the C-terminal domains of the archaeal MCMs of Sulfolobus solfataricus (Sso) and Methanothermobacter thermautotrophicus (Mth). Those domains consist of a structurally conserved truncated winged helix (WH) domain lacking the two typical 'wings' of canonical WH domains. A less conserved N-terminal extension links this WH module to the MCM AAA+ domain forming the ATPase center. In the Sso MCM this linker contains a short alpha-helical element. Using Sso MCM mutants, including chimeric constructs containing Mth C-terminal domain elements, we show that the ATPase and helicase activity of the Sso MCM is significantly modulated by the short alpha-helical linker element and by N-terminal residues of the first alpha-helix of the truncated WH module. Finally, based on our structural and functional data, we present a docking-derived model of the Sso MCM, which implies an allosteric control of the ATPase center by the C-terminal domain.

Structure and regulatory role of the C-terminal winged helix domain of the archaeal minichromosome maintenance complex.,Wiedemann C, Szambowska A, Hafner S, Ohlenschlager O, Guhrs KH, Gorlach M Nucleic Acids Res. 2015 Mar 11;43(5):2958-67. doi: 10.1093/nar/gkv120. Epub 2015 , Feb 20. PMID:25712103^[2]

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

References

↑ Carpentieri F, De Felice M, De Falco M, Rossi M, Pisani FM. Physical and functional interaction between the mini-chromosome maintenance-like DNA helicase and the single-stranded DNA binding protein from the crenarchaeon Sulfolobus solfataricus. J Biol Chem. 2002 Apr 5;277(14):12118-27. Epub 2002 Jan 30. PMID:11821426 doi:10.1074/jbc.M200091200
↑ Wiedemann C, Szambowska A, Hafner S, Ohlenschlager O, Guhrs KH, Gorlach M. Structure and regulatory role of the C-terminal winged helix domain of the archaeal minichromosome maintenance complex. Nucleic Acids Res. 2015 Mar 11;43(5):2958-67. doi: 10.1093/nar/gkv120. Epub 2015 , Feb 20. PMID:25712103 doi:http://dx.doi.org/10.1093/nar/gkv120

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/2m45"

@@ Line 1: / Line 1: @@
 ==NMR solution structure of the C-terminus of the minichromosome maintenance protein MCM from Sulfolobus solfataricus==
 <StructureSection load='2m45' size='340' side='right' caption='[[2m45]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MCM, SSO0774 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273057 SULSO])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </span></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=2m45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m45 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2m45 RCSB], [http://www.ebi.ac.uk/pdbsum/2m45 PDBsum]</span></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=2m45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m45 OCA], [http://pdbe.org/2m45 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2m45 RCSB], [http://www.ebi.ac.uk/pdbsum/2m45 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2m45 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2m45" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

2m45

From Proteopedia

Revision as of 17:29, 9 March 2017

NMR solution structure of the C-terminus of the minichromosome maintenance protein MCM from Sulfolobus solfataricus

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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