1pjr

<table><tr><td colspan='2'>[[1pjr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PJR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1PJR FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PCRA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 ATCC 12980])</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=1pjr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pjr OCA], [http://pdbe.org/1pjr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pjr RCSB], [http://www.ebi.ac.uk/pdbsum/1pjr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pjr ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/PCRA_GEOSE PCRA_GEOSE]] DNA helicase. Has a broad nucleotide specificity, even being able to hydrolyze ethenonucleotides, and is able to couple the hydrolysis to unwinding of DNA substrates. It is a 3'-5' helicase but at high protein concentrations it can also displace a substrate with a 5' tail. Preferred substrate being one with both single and double-stranded regions of DNA.

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== Publication Abstract from PubMed ==

There are a wide variety of helicases that unwind helical DNA and RNA substrates. The twelve helicases that have been identified in Escherichia coli play a role in almost all cellular processes involving nucleic acids. We have solved the crystal structure of a monomeric form of a DNA helicase from Bacillus stearothermophilus, alone and in a complex with ADP, at 2.5 and 2.9 A resolution, respectively. The enzyme comprises two domains with a deep cleft running between them. The ATP-binding site, which is situated at the bottom of this cleft, is formed by motifs that are conserved across the superfamily of related helicases. Unexpected structural homology with the DNA recombination protein, RecA, suggests how ATP binding and hydrolysis may drive conformational changes of the enzyme during catalysis, and implies that there is a common mechanism for all helicases.

Crystal structure of a DExx box DNA helicase.,Subramanya HS, Bird LE, Brannigan JA, Wigley DB Nature. 1996 Nov 28;384(6607):379-83. PMID:8934527<ref>PMID:8934527</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1pjr" style="background-color:#fffaf0;"></div>

*[[Molecular Playground/PcrA Helicase|Molecular Playground/PcrA Helicase]]

*[[PcrA helicase|PcrA helicase]]

== References ==

<references/>

[[Category: Atcc 12980]]

[[Category: Bird, L E]]

[[Category: Brannigan, J A]]

[[Category: Subramanya, H S]]

[[Category: Wigley, D B]]

[[Category: Sos response]]