2g88: Difference between revisions

Revision as of 15:34, 27 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:2g88.png

Template:STRUCTURE 2g88

MSRECA-dATP COMPLEXMSRECA-dATP COMPLEX

Template:ABSTRACT PUBMED 16648362

About this StructureAbout this Structure

2G88 is a Single protein structure of sequence from Mycobacterium smegmatis. Full crystallographic information is available from OCA.

ReferenceReference

Crystallographic identification of an ordered C-terminal domain and a second nucleotide-binding site in RecA: new insights into allostery., Krishna R, Manjunath GP, Kumar P, Surolia A, Chandra NR, Muniyappa K, Vijayan M, Nucleic Acids Res. 2006 Apr 28;34(8):2186-95. Print 2006. PMID:16648362

Crystal structures of Mycobacterium tuberculosis RecA and its complex with ADP-AlF(4): implications for decreased ATPase activity and molecular aggregation., Datta S, Prabu MM, Vaze MB, Ganesh N, Chandra NR, Muniyappa K, Vijayan M, Nucleic Acids Res. 2000 Dec 15;28(24):4964-73. PMID:11121488

Structural studies on MtRecA-nucleotide complexes: insights into DNA and nucleotide binding and the structural signature of NTP recognition., Datta S, Ganesh N, Chandra NR, Muniyappa K, Vijayan M, Proteins. 2003 Feb 15;50(3):474-85. PMID:12557189

Crystal structures of Mycobacterium smegmatis RecA and its nucleotide complexes., Datta S, Krishna R, Ganesh N, Chandra NR, Muniyappa K, Vijayan M, J Bacteriol. 2003 Jul;185(14):4280-4. PMID:12837805

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OCA

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 {{STRUCTURE_2g88|  PDB=2g88  |  SCENE=  }}
-'''MSRECA-dATP COMPLEX'''
+===MSRECA-dATP COMPLEX===
-==Overview==
+<!--
-RecA protein is a crucial and central component of the homologous recombination and DNA repair machinery. Despite numerous studies on the protein, several issues concerning its action, including the allosteric regulation mechanism have remained unclear. Here we report, for the first time, a crystal structure of a complex of Mycobacterium smegmatis RecA (MsRecA) with dATP, which exhibits a fully ordered C-terminal domain, with a second dATP molecule bound to it. ATP binding is an essential step for all activities of RecA, since it triggers the formation of active nucleoprotein filaments. In the crystal filament, dATP at the first site communicates with a dATP of the second site of an adjacent subunit, through conserved residues, suggesting a new route for allosteric regulation. In addition, subtle but definite changes observed in the orientation of the nucleotide at the first site and in the positions of the segment preceding loop L2 as well as in the segment 102-105 situated between the 2 nt, all appear to be concerted and suggestive of a biological role for the second bound nucleotide.
+The line below this paragraph, {{ABSTRACT_PUBMED_16648362}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16648362 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16648362}}
 ==About this Structure==
@@ Line 20: / Line 24: @@
 ==Reference==
 Crystallographic identification of an ordered C-terminal domain and a second nucleotide-binding site in RecA: new insights into allostery., Krishna R, Manjunath GP, Kumar P, Surolia A, Chandra NR, Muniyappa K, Vijayan M, Nucleic Acids Res. 2006 Apr 28;34(8):2186-95. Print 2006. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16648362 16648362]
+Crystal structures of Mycobacterium tuberculosis RecA and its complex with ADP-AlF(4): implications for decreased ATPase activity and molecular aggregation., Datta S, Prabu MM, Vaze MB, Ganesh N, Chandra NR, Muniyappa K, Vijayan M, Nucleic Acids Res. 2000 Dec 15;28(24):4964-73. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11121488 11121488]
+Structural studies on MtRecA-nucleotide complexes: insights into DNA and nucleotide binding and the structural signature of NTP recognition., Datta S, Ganesh N, Chandra NR, Muniyappa K, Vijayan M, Proteins. 2003 Feb 15;50(3):474-85. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12557189 12557189]
+Crystal structures of Mycobacterium smegmatis RecA and its nucleotide complexes., Datta S, Krishna R, Ganesh N, Chandra NR, Muniyappa K, Vijayan M, J Bacteriol. 2003 Jul;185(14):4280-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12837805 12837805]
 [[Category: Mycobacterium smegmatis]]
 [[Category: Single protein]]
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 [[Category: Dna-repair]]
 [[Category: Recombination]]
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