1g19

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[[Image:1g19.gif|left|200px]]
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{{Structure
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|PDB= 1g19 |SIZE=350|CAPTION= <scene name='initialview01'>1g19</scene>, resolution 3.00&Aring;
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The line below this paragraph, containing "STRUCTURE_1g19", creates the "Structure Box" on the page.
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Deleted_entry Deleted entry], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.99.37 3.4.99.37] </span>
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|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam00154 RecA], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd00983 recA]</span>
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{{STRUCTURE_1g19| PDB=1g19 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g19 OCA], [http://www.ebi.ac.uk/pdbsum/1g19 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g19 RCSB]</span>
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'''STRUCTURE OF RECA PROTEIN'''
'''STRUCTURE OF RECA PROTEIN'''
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Revision as of 14:00, 2 May 2008

Image:1g19.gif

Template:STRUCTURE 1g19

STRUCTURE OF RECA PROTEIN


Overview

Sequencing of the complete genome of Mycobacterium tuberculosis, combined with the rapidly increasing need to improve tuberculosis management through better drugs and vaccines, has initiated extensive research on several key proteins from the pathogen. RecA, a ubiquitous multifunctional protein, is a key component of the processes of homologous genetic recombination and DNA repair. Structural knowledge of MtRecA is imperative for a full understanding of both these activities and any ensuing application. The crystal structure of MtRecA, presented here, has six molecules in the unit cell forming a 6(1) helical filament with a deep groove capable of binding DNA. The observed weakening in the higher order aggregation of filaments into bundles may have implications for recombination in mycobacteria. The structure of the complex reveals the atomic interactions of ADP-AlF(4), an ATP analogue, with the P-loop-containing binding pocket. The structures explain reduced levels of interactions of MtRecA with ATP, despite sharing the same fold, topology and high sequence similarity with EcRecA. The formation of a helical filament with a deep groove appears to be an inherent property of MtRecA. The histidine in loop L1 appears to be positioned appropriately for DNA interaction.

About this Structure

1G19 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Fri May 2 17:00:25 2008

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