4oxx: Difference between revisions
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==Crystal Structure of Cindoxin, Surface Entropy reduction Mutant== | |||
<StructureSection load='4oxx' size='340' side='right' caption='[[4oxx]], [[Resolution|resolution]] 1.21Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4oxx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_51113 Atcc 51113]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OXX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OXX FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cinC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=57706 ATCC 51113])</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4oxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oxx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oxx RCSB], [http://www.ebi.ac.uk/pdbsum/4oxx PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structure of the flavin mononucleotide (FMN)-containing redox partner to P450cin, cindoxin (Cdx), has been determined to 1.3 A resolution. The overall structure is similar to that of the FMN domain of human cytochrome P450 reductase. A Brownian dynamics-molecular dynamics docking method was used to produce a model of Cdx with its redox partner, P450cin. This Cdx-P450cin model highlights the potential importance of Cdx Tyr96 in bridging the FMN and heme cofactors as well P450cin Arg102 and Arg346. Each of the single-site Ala mutants exhibits approximately 10% of the wild-type activity, thus demonstrating the importance of these residues for binding and/or electron transfer. In the well-studied P450cam system, redox partner binding stabilizes the open low-spin conformation of P450cam and greatly decreases the stability of the oxy complex. In sharp contrast, Cdx does not shift P450cin to a low-spin state, although the stability of oxy-P450cin is decreased 10-fold in the presence of Cdx. This indicates that Cdx may have a modest effect on the open-closed equilibrium in P450cin compared to that in P450cam. It has been postulated that part of the effector role of Pdx on P450cam is to promote a significant structural change that makes available a proton relay network involving Asp251 required for O2 activation. The structure around the corresponding Asp in P450cin, Asp241, provides a possible structural reason for why P450cin is less dependent on its redox partner for functionally important structural changes. | |||
Crystal structure of cindoxin, the p450cin redox partner.,Madrona Y, Hollingsworth SA, Tripathi S, Fields JB, Rwigema JC, Tobias DJ, Poulos TL Biochemistry. 2014 Mar 11;53(9):1435-46. doi: 10.1021/bi500010m. Epub 2014 Feb, 25. PMID:24533927<ref>PMID:24533927</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Atcc 51113]] | |||
[[Category: Madrona, Y.]] | [[Category: Madrona, Y.]] | ||
[[Category: Poulos, T L.]] | [[Category: Poulos, T L.]] | ||