4kpb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
{{STRUCTURE_4kpb| PDB=4kpb | SCENE= }}
+
==Crystal structure of cytochrome P450 BM-3 R47E mutant==
-
===Crystal structure of cytochrome P450 BM-3 R47E mutant===
+
<StructureSection load='4kpb' size='340' side='right' caption='[[4kpb]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
-
{{ABSTRACT_PUBMED_23829560}}
+
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[4kpb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KPB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KPB FirstGlance]. <br>
 +
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
 +
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kpa|4kpa]]</td></tr>
 +
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cyp102A1, cyp102 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 Bacillus megaterium])</td></tr>
 +
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] </span></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=4kpb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kpb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kpb RCSB], [http://www.ebi.ac.uk/pdbsum/4kpb PDBsum]</span></td></tr>
 +
</table>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Cytochrome P450 BM-3 is a bacterial enzyme with sequence similarity to mammalian P450s that catalyzes the hydroxylation of fatty acids with high efficiency. Enzyme-substrate binding and dynamics has been an important topic of study in cytochromes P450, since most of the crystal structures published show the substrate in an inactive state. We have determined a new crystal structure of cytochrome P450 BM-3 in complex with N-palmitoylglycine (NPG), which unexpectedly showed a direct bidentate ion-pair between NPG and arginine 47 (R47). We further explored the role of R47, the only charged residue in the binding pocket in cytochrome P450 BM-3, through mutagenesis and crystallographic studies. The mutations of R47 to glutamine (R47Q), glutamic acid (R47E), and lysine (R47K) were designed to investigate the role of this residue's charge in binding and catalysis. The oppositely charged R47E mutation had the greatest effect on activity and binding. The crystal structure of R47E BMP shows that the glutamic acid side chain is blocking the entrance to the binding pocket, accounting for NPG's low binding affinity and charge repulsion. For R47Q and R47K BM-3, the mutations caused only a slight change in kcat and a large change in Km and Kd, which suggests that R47 mostly is involved in binding and that our crystal structure represents an initial binding step in the P450 cycle.
-
==Function==
+
Structural Evidence: A Single Charged Residue Affects Substrate Binding in Cytochrome P450 BM-3.,Catalano J, Sadre-Bazzaz K, Amodeo GA, Tong L, McDermott AE Biochemistry. 2013 Jul 6. PMID:23829560<ref>PMID:23829560</ref>
-
[[http://www.uniprot.org/uniprot/CPXB_BACME CPXB_BACME]] Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of medium and long-chain fatty acids at omega-1, omega-2 and omega-3 positions, with optimum chain lengths of 12-16 carbons (lauric, myristic, and palmitic acids). The reductase domain is required for electron transfer from NADP to cytochrome P450.
+
-
==About this Structure==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[4kpb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KPB OCA].
+
</div>
==See Also==
==See Also==
*[[Cytochrome P450|Cytochrome P450]]
*[[Cytochrome P450|Cytochrome P450]]
-
*[[NADPH-Cytochrome P450 Reductase|NADPH-Cytochrome P450 Reductase]]
+
== References ==
-
 
+
<references/>
-
==Reference==
+
__TOC__
-
<ref group="xtra">PMID:023829560</ref><references group="xtra"/><references/>
+
</StructureSection>
[[Category: Bacillus megaterium]]
[[Category: Bacillus megaterium]]
[[Category: Unspecific monooxygenase]]
[[Category: Unspecific monooxygenase]]
-
[[Category: Catalano, J.]]
+
[[Category: Catalano, J]]
-
[[Category: McDermott, A E.]]
+
[[Category: McDermott, A E]]
-
[[Category: Sadre-Bazzaz, K.]]
+
[[Category: Sadre-Bazzaz, K]]
-
[[Category: Tong, L.]]
+
[[Category: Tong, L]]
[[Category: Heme-dependent stereospecific oxidation of substrate]]
[[Category: Heme-dependent stereospecific oxidation of substrate]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]

Revision as of 15:20, 21 December 2014

Crystal structure of cytochrome P450 BM-3 R47E mutant

4kpb, resolution 2.10Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools