3pjr: Difference between revisions

Revision as of 13:02, 3 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:3pjr.png

3pjr, resolution 3.30Å ()

Ligands:

Structural annotation:
Resources:	CATH : 3Pjra03, 3Pjra04, 3Pjra01, 3Pjra02 InterPro : Ipr013986, Ipr014016, Ipr005751, Ipr000212, Ipr014017 Pfam : PF00580 SCOP : d3pjra1, d3pjra2

Evolutionary conservation:

Toggle Conservation Colors:

Rows = identical sequences:

Further Information:

Caveats,

Explanation,
Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, RCSB, PDBsum

Coordinates:

save as pdb, mmCIF, xml

HELICASE SUBSTRATE COMPLEXHELICASE SUBSTRATE COMPLEX

Template:ABSTRACT PUBMED 10199404

About this StructureAbout this Structure

3PJR is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism., Velankar SS, Soultanas P, Dillingham MS, Subramanya HS, Wigley DB, Cell. 1999 Apr 2;97(1):75-84. PMID:10199404

Page seeded by OCA on Thu Jul 3 13:02:34 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-==Overview==
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-We have determined two different structures of PcrA DNA helicase complexed with the same single strand tailed DNA duplex, providing snapshots of different steps on the catalytic pathway. One of the structures is of a complex with a nonhydrolyzable analog of ATP and is thus a "substrate" complex. The other structure contains a bound sulphate ion that sits in a position equivalent to that occupied by the phosphate ion produced after ATP hydrolysis, thereby mimicking a "product" complex. In both complexes, the protein is monomeric. Large and distinct conformational changes occur on binding DNA and the nucleotide cofactor. Taken together, these structures provide evidence against an "active rolling" model for helicase action but are instead consistent with an "inchworm" mechanism.
+The line below this paragraph, {{ABSTRACT_PUBMED_10199404}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10199404 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10199404}}
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 [[Category: Wigley, D B.]]
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