4ppf: Difference between revisions
New page: '''Unreleased structure''' The entry 4ppf is ON HOLD Authors: Chandran, A.V., Prabu, J.R., Patil, N.K., Muniyappa, K., Vijayan, M. Description: Mycobacterium tuberculosis RecA citrate ... |
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The | ==Mycobacterium tuberculosis RecA citrate bound low temperature structure IIA-N== | ||
<StructureSection load='4ppf' size='340' side='right'caption='[[4ppf]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ppf]] 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=4PPF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PPF FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=4ppf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ppf OCA], [https://pdbe.org/4ppf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ppf RCSB], [https://www.ebi.ac.uk/pdbsum/4ppf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ppf ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[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] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Structures of crystals of Mycobacterium tuberculosis RecA, grown and analysed under different conditions, provide insights into hitherto underappreciated details of molecular structure and plasticity. In particular, they yield information on the invariant and variable features of the geometry of the P-loop, whose binding to ATP is central for all the biochemical activities of RecA. The strengths of interaction of the ligands with the P-loop reveal significant differences. This in turn affects the magnitude of the motion of the 'switch' residue, Gln195 in M. tuberculosis RecA, which triggers the transmission of ATP-mediated allosteric information to the DNA binding region. M. tuberculosis RecA is substantially rigid compared with its counterparts from M. smegmatis and E. coli, which exhibit concerted internal molecular mobility. The interspecies variability in the plasticity of the two mycobacterial proteins is particularly surprising as they have similar sequence and 3D structure. Details of the interactions of ligands with the protein, characterized in the structures reported here, could be useful for design of inhibitors against M. tuberculosis RecA. | |||
Structural studies on Mycobacterium tuberculosis RecA: Molecular plasticity and interspecies variability.,Chandran AV, Prabu JR, Nautiyal A, Patil KN, Muniyappa K, Vijayan M J Biosci. 2015 Mar;40(1):13-30. PMID:25740138<ref>PMID:25740138</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4ppf" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[3D structures of recombinase A|3D structures of recombinase A]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mycobacterium tuberculosis]] | |||
[[Category: Chandran AV]] | |||
[[Category: Muniyappa K]] | |||
[[Category: Patil NK]] | |||
[[Category: Prabu JR]] | |||
[[Category: Vijayan M]] | |||
Latest revision as of 18:00, 8 November 2023
Mycobacterium tuberculosis RecA citrate bound low temperature structure IIA-NMycobacterium tuberculosis RecA citrate bound low temperature structure IIA-N
Structural highlights
FunctionRECA_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] Publication Abstract from PubMedStructures of crystals of Mycobacterium tuberculosis RecA, grown and analysed under different conditions, provide insights into hitherto underappreciated details of molecular structure and plasticity. In particular, they yield information on the invariant and variable features of the geometry of the P-loop, whose binding to ATP is central for all the biochemical activities of RecA. The strengths of interaction of the ligands with the P-loop reveal significant differences. This in turn affects the magnitude of the motion of the 'switch' residue, Gln195 in M. tuberculosis RecA, which triggers the transmission of ATP-mediated allosteric information to the DNA binding region. M. tuberculosis RecA is substantially rigid compared with its counterparts from M. smegmatis and E. coli, which exhibit concerted internal molecular mobility. The interspecies variability in the plasticity of the two mycobacterial proteins is particularly surprising as they have similar sequence and 3D structure. Details of the interactions of ligands with the protein, characterized in the structures reported here, could be useful for design of inhibitors against M. tuberculosis RecA. Structural studies on Mycobacterium tuberculosis RecA: Molecular plasticity and interspecies variability.,Chandran AV, Prabu JR, Nautiyal A, Patil KN, Muniyappa K, Vijayan M J Biosci. 2015 Mar;40(1):13-30. PMID:25740138[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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