2a7z: Difference between revisions

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 {{Theoretical_model}}
-{{Seed}}
-[[Image:2a7z.png|left|200px]]
-<!--
+==MOLECULAR MODEL OF RECX==
-The line below this paragraph, containing "STRUCTURE_2a7z", creates the "Structure Box" on the page.
+<StructureSection load='2a7z' size='340' side='right'caption='[[2a7z]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A7Z FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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=2a7z FirstGlance], [https://www.ebi.ac.uk/pdbsum/2a7z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a7z ProSAT]</span></td></tr>
--->
+</table>
-{{STRUCTURE_2a7z|  PDB=2a7z  |  SCENE=  }}
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The protein RecA is involved in homologous recombination, DNA repair and also catalyzes DNA strand exchange. RecX gene is downstream of recA and the gene product RecX is supposed to be important for RecA regulation. Recombinant RecX is purified to homogeneity, and circular dichroism (CD) and FTIR spectroscopy show the protein to exist mostly in helical conformation. The fluorescence emission maxima of the native and the denatured protein and the steady-state fluorescence quenching studies with acrylamide indicate the presence of tryptophan residues partially exposed to the bulk solvent. Denaturation studies with urea and guanidine hydrochloride by use of spectroscopic methods, fluorescence, and CD also confirm the instability of the protein and unfolding occurs following a two-state model. Mass spectrometry and gel permeation chromatography suggest the monomeric form of the protein. Molecular modeling of RecX represents the molecule as extended and helical bundle in conformity with the spectroscopic results. To understand the mechanism of RecX in the regulation of RecA the structural model of RecA-RecX has been discussed. In this proposed model, entry of RecX into hexameric RecA filament prevents binding of ssDNA and also inhibits ATPase activity.
-===MOLECULAR MODEL OF RECX===
+Molecular modeling of RecX reveals its mode of interaction with RecA.,Mishra S, Mazumdar PA, Dey J, Das AK Biochem Biophys Res Commun. 2003 Dec 19;312(3):615-22. PMID:14680809<ref>PMID:14680809</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_14680809}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2a7z" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 14680809 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_14680809}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Theoretical Model]]
-Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A7Z OCA].
+[[Category: Large Structures]]
-==Reference==
-<ref group="xtra">PMID:14680809</ref><references group="xtra"/>
 [[Category: Das, A K]]
 [[Category: Dey, J]]
 [[Category: Mazumdar, P A]]
 [[Category: Mishra, S]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr  8 07:39:31 2010''