2odn: Difference between revisions

Revision as of 16:09, 28 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:2odn.png

Template:STRUCTURE 2odn

MSRECA-dATP complexMSRECA-dATP complex

Template:ABSTRACT PUBMED 17306300

About this StructureAbout this Structure

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

ReferenceReference

Snapshots of RecA protein involving movement of the C-domain and different conformations of the DNA-binding loops: crystallographic and comparative analysis of 11 structures of Mycobacterium smegmatis RecA., Krishna R, Prabu JR, Manjunath GP, Datta S, Chandra NR, Muniyappa K, Vijayan M, J Mol Biol. 2007 Apr 6;367(4):1130-44. Epub 2007 Jan 26. PMID:17306300

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

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

Page seeded by OCA on Mon Jul 28 16:09:28 2008

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OCA

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-[[Image:2odn.jpg|left|200px]]
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 {{STRUCTURE_2odn|  PDB=2odn  |  SCENE=  }}
-'''MSRECA-dATP complex'''
+===MSRECA-dATP complex===
-==Overview==
+<!--
-Mycobacterium smegmatis RecA and its nucleotide complexes crystallize in three different, but closely related, forms characterized by specific ranges of unit cell dimensions. The six crystals reported here and five reported earlier, all grown under the same or very similar conditions, belong to these three forms, all in space group P6(1). They include one obtained by reducing relative humidity around the crystal. In all crystals, RecA monomers form filaments around a 6(1) screw axis. Thus, the c-dimension of the crystal corresponds to the pitch of the RecA filament. As reported for Escherichia coli RecA, the variation in the pitch among the three forms correlates well with the motion of the C-terminal domain of the RecA monomers with respect to the main domain. The domain motion is compatible with formation of inactive as well as active RecA filaments involving monomers with a fully ordered C domain. It does not appear to influence the movement upon nucleotide-binding of the switch residue, which is believed to provide the trigger for transmitting the effect of nucleotide binding to the DNA-binding region. Interestingly, partial dehydration of the crystal results in the movement of the residue similar to that caused by nucleotide binding. The ordering of the DNA-binding loops, which present ensembles of conformations, is also unaffected by domain motion. The conformation of loop L2 appears to depend upon nucleotide binding, presumably on account of the movement of the switch residue that forms part of the loop. The conformations of loops L1 and L2 are correlated and have implications for intermolecular communications within the RecA filament. The structures resulting from different orientations of the C domain and different conformations of the DNA-binding loops appear to represent snapshots of the RecA at different phases of activity, and provide insights into the mechanism of action of RecA.
+The line below this paragraph, {{ABSTRACT_PUBMED_17306300}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17306300 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17306300}}
 ==About this Structure==
@@ Line 20: / Line 24: @@
 ==Reference==
 Snapshots of RecA protein involving movement of the C-domain and different conformations of the DNA-binding loops: crystallographic and comparative analysis of 11 structures of Mycobacterium smegmatis RecA., Krishna R, Prabu JR, Manjunath GP, Datta S, Chandra NR, Muniyappa K, Vijayan M, J Mol Biol. 2007 Apr 6;367(4):1130-44. Epub 2007 Jan 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17306300 17306300]
+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]
+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]
 [[Category: Deleted entry]]
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