2vl6: Difference between revisions
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{{STRUCTURE_2vl6| PDB=2vl6 | SCENE= }} | {{STRUCTURE_2vl6| PDB=2vl6 | SCENE= }} | ||
===STRUCTURAL ANALYSIS OF THE SULFOLOBUS SOLFATARICUS MCM PROTEIN N- TERMINAL DOMAIN=== | |||
{{ABSTRACT_PUBMED_18417534}} | |||
=== | ==Function== | ||
[[http://www.uniprot.org/uniprot/MCM_SULSO 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.<ref>PMID:11821426</ref> | |||
==About this Structure== | ==About this Structure== | ||
[[2vl6]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/ | [[2vl6]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35091 Atcc 35091]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VL6 OCA]. | ||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:018417534</ref><references group="xtra"/> | <ref group="xtra">PMID:018417534</ref><references group="xtra"/><references/> | ||
[[Category: | [[Category: Atcc 35091]] | ||
[[Category: Ladenstein, R.]] | [[Category: Ladenstein, R.]] | ||
[[Category: Liu, W.]] | [[Category: Liu, W.]] | ||
Revision as of 06:17, 4 December 2013
STRUCTURAL ANALYSIS OF THE SULFOLOBUS SOLFATARICUS MCM PROTEIN N- TERMINAL DOMAIN
Template:ABSTRACT PUBMED 18417534
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]
About this Structure
2vl6 is a 3 chain structure with sequence from Atcc 35091. Full crystallographic information is available from OCA.
Reference
- Liu W, Pucci B, Rossi M, Pisani FM, Ladenstein R. Structural analysis of the Sulfolobus solfataricus MCM protein N-terminal domain. Nucleic Acids Res. 2008 Jun;36(10):3235-43. Epub 2008 Apr 16. PMID:18417534 doi:10.1093/nar/gkn183
- ↑ 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
