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| | <StructureSection load='1g19' size='340' side='right'caption='[[1g19]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='1g19' size='340' side='right'caption='[[1g19]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1g19]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G19 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G19 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1g19]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G19 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1g19 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g19 RCSB], [http://www.ebi.ac.uk/pdbsum/1g19 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1g19 ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1g19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g19 OCA], [https://pdbe.org/1g19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g19 RCSB], [https://www.ebi.ac.uk/pdbsum/1g19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g19 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RECA_MYCTU RECA_MYCTU]] Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.[HAMAP-Rule:MF_00268] PI-MtuI is an endonuclease.[HAMAP-Rule:MF_00268] | + | [https://www.uniprot.org/uniprot/RECA_MYCTU RECA_MYCTU] Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.[HAMAP-Rule:MF_00268] PI-MtuI is an endonuclease.[HAMAP-Rule:MF_00268] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Recombinase A|Recombinase A]] | + | *[[3D structures of recombinase A|3D structures of recombinase A]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Mycobacterium tuberculosis]] | | [[Category: Mycobacterium tuberculosis]] |
| - | [[Category: Chandra, N R]] | + | [[Category: Chandra NR]] |
| - | [[Category: Datta, S]] | + | [[Category: Datta S]] |
| - | [[Category: Ganesh, N]] | + | [[Category: Ganesh N]] |
| - | [[Category: Muniyappa, K]] | + | [[Category: Muniyappa K]] |
| - | [[Category: Prabu, M M]] | + | [[Category: Prabu MM]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Vaze MB]] |
| - | [[Category: Vaze, M B]] | + | [[Category: Vijayan M]] |
| - | [[Category: Vijayan, M]] | + | |
| - | [[Category: Dna-repair]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| - | [[Category: Recombination]]
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| - | [[Category: Tbsgc]]
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| Structural highlights
Function
RECA_MYCTU Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.[HAMAP-Rule:MF_00268] PI-MtuI is an endonuclease.[HAMAP-Rule:MF_00268]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Datta S, Prabu MM, Vaze MB, Ganesh N, Chandra NR, Muniyappa K, Vijayan M. Crystal structures of Mycobacterium tuberculosis RecA and its complex with ADP-AlF(4): implications for decreased ATPase activity and molecular aggregation. Nucleic Acids Res. 2000 Dec 15;28(24):4964-73. PMID:11121488
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