8yb2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:19, 12 February 2025) (edit) (undo)
 
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 8yb2 is ON HOLD
+
==XFEL crystal structure of the oxygen-bound form of F393H P450BM3 with N-enanthyl-L-prolyl-L-phenylalanine in complex with styrene==
-
 
+
<StructureSection load='8yb2' size='340' side='right'caption='[[8yb2]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
-
Authors: Nagao, S., Kuwano, W., Tosha, T., Yamashita, K., Stanfield, J.K., Kasai, C., Ariyasu, S., Shoji, O., Sugimoto, H., Kubo, M.
+
== Structural highlights ==
-
 
+
<table><tr><td colspan='2'>[[8yb2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Priestia_megaterium_NBRC_15308_=_ATCC_14581 Priestia megaterium NBRC 15308 = ATCC 14581]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8YB2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8YB2 FirstGlance]. <br>
-
Description: XFEL crystal structure of the oxygen-bound form of F393H P450BM3 with N-enanthyl-L-prolyl-L-phenylalanine in complex with styrene
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
-
[[Category: Unreleased Structures]]
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D0L:(2~{S})-2-[[(2~{S})-1-heptylpyrrolidin-2-yl]carbonylamino]-3-phenyl-propanoic+acid'>D0L</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=SYN:ETHENYLBENZENE'>SYN</scene></td></tr>
-
[[Category: Nagao, S]]
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8yb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8yb2 OCA], [https://pdbe.org/8yb2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8yb2 RCSB], [https://www.ebi.ac.uk/pdbsum/8yb2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8yb2 ProSAT]</span></td></tr>
-
[[Category: Stanfield, J.K]]
+
</table>
-
[[Category: Tosha, T]]
+
== Function ==
-
[[Category: Kubo, M]]
+
[https://www.uniprot.org/uniprot/CPXB_PRIM2 CPXB_PRIM2] Functions as a fatty acid monooxygenase (PubMed:11695892, PubMed:14653735, PubMed:16403573, PubMed:16566047, PubMed:17077084, PubMed:1727637, PubMed:17868686, PubMed:18004886, PubMed:18298086, PubMed:18619466, PubMed:18721129, PubMed:19492389, PubMed:20180779, PubMed:21110374, PubMed:21875028, PubMed:3106359, PubMed:7578081). Catalyzes hydroxylation of fatty acids at omega-1, omega-2 and omega-3 positions (PubMed:1727637, PubMed:21875028). Shows activity toward medium and long-chain fatty acids, with optimum chain lengths of 12, 14 and 16 carbons (lauric, myristic, and palmitic acids). Able to metabolize some of these primary metabolites to secondary and tertiary products (PubMed:1727637). Marginal activity towards short chain lengths of 8-10 carbons (PubMed:1727637, PubMed:18619466). Hydroxylates highly branched fatty acids, which play an essential role in membrane fluidity regulation (PubMed:16566047). Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain (PubMed:11695892, PubMed:14653735, PubMed:16403573, PubMed:16566047, PubMed:17077084, PubMed:1727637, PubMed:17868686, PubMed:18004886, PubMed:18298086, PubMed:18619466, PubMed:18721129, PubMed:19492389, PubMed:20180779, PubMed:21110374, PubMed:21875028, PubMed:3106359, PubMed:7578081). Involved in inactivation of quorum sensing signals of other competing bacteria by oxidazing efficiently acyl homoserine lactones (AHLs), molecules involved in quorum sensing signaling pathways, and their lactonolysis products acyl homoserines (AHs) (PubMed:18020460).<ref>PMID:11695892</ref> <ref>PMID:14653735</ref> <ref>PMID:16403573</ref> <ref>PMID:16566047</ref> <ref>PMID:17077084</ref> <ref>PMID:1727637</ref> <ref>PMID:17868686</ref> <ref>PMID:18004886</ref> <ref>PMID:18020460</ref> <ref>PMID:18298086</ref> <ref>PMID:18619466</ref> <ref>PMID:18721129</ref> <ref>PMID:19492389</ref> <ref>PMID:20180779</ref> <ref>PMID:21110374</ref> <ref>PMID:21875028</ref> <ref>PMID:3106359</ref> <ref>PMID:7578081</ref>
-
[[Category: Sugimoto, H]]
+
== References ==
-
[[Category: Ariyasu, S]]
+
<references/>
-
[[Category: Yamashita, K]]
+
__TOC__
-
[[Category: Kasai, C]]
+
</StructureSection>
-
[[Category: Shoji, O]]
+
[[Category: Large Structures]]
-
[[Category: Kuwano, W]]
+
[[Category: Priestia megaterium NBRC 15308 = ATCC 14581]]
 +
[[Category: Ariyasu S]]
 +
[[Category: Kasai C]]
 +
[[Category: Kubo M]]
 +
[[Category: Kuwano W]]
 +
[[Category: Nagao S]]
 +
[[Category: Shoji O]]
 +
[[Category: Stanfield JK]]
 +
[[Category: Sugimoto H]]
 +
[[Category: Tosha T]]
 +
[[Category: Yamashita K]]

Current revision

XFEL crystal structure of the oxygen-bound form of F393H P450BM3 with N-enanthyl-L-prolyl-L-phenylalanine in complex with styrene

PDB ID 8yb2

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/8yb2"
Personal tools