This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4psk

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 01:07, 16 November 2017

Mycobacterium tuberculosis RecA phosphate bound low temperature structure I-LT

Structural highlights

4psk is a 1 chain structure with sequence from "bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	4oqf, 4po1, 4po8, 4po9, 4poa, 4ppf, 4ppg, 4ppn, 4ppq, 4pqf, 4pqr, 4pqy, 4pr0, 4psa, 4psv, 4ptl
Gene:	MT2806, MTV002.02c, recA, Rv2737c ("Bacillus tuberculosis" (Zopf 1883) Klein 1884)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Chandran AV, Prabu JR, Nautiyal A, Patil KN, Muniyappa K, Vijayan M. Structural studies on Mycobacterium tuberculosis RecA: Molecular plasticity and interspecies variability. J Biosci. 2015 Mar;40(1):13-30. PMID:25740138

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4psk"

@@ Line 3: / Line 3: @@
 <StructureSection load='4psk' size='340' side='right' caption='[[4psk]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4psk]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PSK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PSK FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4psk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PSK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PSK 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>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4oqf|4oqf]], [[4po1|4po1]], [[4po8|4po8]], [[4po9|4po9]], [[4poa|4poa]], [[4ppf|4ppf]], [[4ppg|4ppg]], [[4ppn|4ppn]], [[4ppq|4ppq]], [[4pqf|4pqf]], [[4pqr|4pqr]], [[4pqy|4pqy]], [[4pr0|4pr0]], [[4psa|4psa]], [[4psv|4psv]], [[4ptl|4ptl]]</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MT2806, MTV002.02c, recA, Rv2737c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</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=4psk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4psk OCA], [http://pdbe.org/4psk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4psk RCSB], [http://www.ebi.ac.uk/pdbsum/4psk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4psk ProSAT]</span></td></tr>
 </table>
@@ Line 19: / Line 20: @@
 </div>
 <div class="pdbe-citations 4psk" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Recombinase A|Recombinase A]]
 == References ==
 <references/>

4psk

From Proteopedia

Revision as of 01:07, 16 November 2017

Mycobacterium tuberculosis RecA phosphate bound low temperature structure I-LT

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox