7ttp - Revision history

OCA at 14:42, 13 August 2026

2026-08-13T14:42:56Z

← Older revision		Revision as of 14:42, 13 August 2026
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	<StructureSection load='7ttp' size='340' side='right'caption='[[7ttp]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='7ttp' size='340' side='right'caption='[[7ttp]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>~~[[7ttp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinomadura_parvosata_subsp._kistnae Actinomadura parvosata subsp. kistnae].~~ Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TTP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TTP FirstGlance]. <br>		<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TTP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TTP FirstGlance]. <br>
	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.8Å</td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.8Å</td></tr>
	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=7ttp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ttp OCA], [https://pdbe.org/7ttp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ttp RCSB], [https://www.ebi.ac.uk/pdbsum/7ttp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ttp ProSAT]</span></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=7ttp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ttp OCA], [https://pdbe.org/7ttp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ttp RCSB], [https://www.ebi.ac.uk/pdbsum/7ttp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ttp ProSAT]</span></td></tr>
	</table>		</table>
	== ~~Function~~ ==		<div style="background-color:#fffaf0;">
	~~[https~~://~~www~~.~~uniprot~~.~~org~~/~~uniprot~~/~~A0A2P9IBF7_9ACTN A0A2P9IBF7_9ACTN]~~		== Publication Abstract from PubMed ==
			Cytochrome P450 enzymes (P450s) are a superfamily of monooxygenases that utilize a cysteine thiolate-ligated heme moiety to perform a wide range of demanding oxidative transformations. Given the oxidative power of the active intermediate formed within P450s during their active cycle, it is remarkable that these enzymes can avoid auto-oxidation and retain the axial cysteine ligand in the deprotonated-and thus highly acidic-thiolate form. While little is known about the process of heme incorporation during P450 folding, there is an overwhelming preference for one heme orientation within the P450 active site. Indeed, very few structures to date contain an alternate heme orientation, of which two are OxyA homologs from glycopeptide antibiotic (GPA) biosynthesis. Given the apparent preference for the unusual heme orientation shown by OxyA enzymes, we investigated the OxyA homolog from kistamicin biosynthesis (OxyAkis), which is an atypical GPA. We determined that OxyAkis is highly sensitive to oxidative damage by peroxide, with both UV and EPR measurements showing rapid bleaching of the heme signal. We determined the structure of OxyAkis and found a mixed population of heme orientations present in this enzyme. Our analysis further revealed the possible modification of the heme moiety, which was only present in samples where the alternate heme orientation was present in the protein. These results suggest that the typical heme orientation in cytochrome P450s can help prevent potential damage to the heme-and hence deactivation of the enzyme-during P450 catalysis. It also suggests that some P450 enzymes involved in GPA biosynthesis may be especially prone to oxidative damage due to the heme orientation found in their active sites.

			The Cytochrome P450 OxyA from the Kistamicin Biosynthesis Cyclization Cascade is Highly Sensitive to Oxidative Damage.,Greule A, Izore T, Machell D, Hansen MH, Schoppet M, De Voss JJ, Charkoudian LK, Schittenhelm RB, Harmer JR, Cryle MJ Front Chem. 2022 Apr 8;10:868240. doi: 10.3389/fchem.2022.868240. eCollection, 2022. PMID:35464232<ref>PMID:35464232</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 7ttp" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Cytochrome P450 hydroxylase 3D structures\|Cytochrome P450 hydroxylase 3D structures]]		*[[Cytochrome P450 hydroxylase 3D structures\|Cytochrome P450 hydroxylase 3D structures]]
			== References ==
			<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	~~[[Category: Actinomadura parvosata subsp. kistnae]]~~
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Cryle MJ]]		[[Category: Cryle MJ]]
	[[Category: Greule A]]		[[Category: Greule A]]
	[[Category: Izore T]]		[[Category: Izore T]]

OCA at 10:56, 21 February 2024

2024-02-21T10:56:27Z

← Older revision		Revision as of 10:56, 21 February 2024
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	==P450 (OxyA) from kistamicin biosynthesis, mixed heme conformation==		==P450 (OxyA) from kistamicin biosynthesis, mixed heme conformation==
	<StructureSection load='7ttp' size='340' side='right'caption='[[7ttp]]' scene=''>		<StructureSection load='7ttp' size='340' side='right'caption='[[7ttp]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TTP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TTP FirstGlance]. <br>		<table><tr><td colspan='2'>[[7ttp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinomadura_parvosata_subsp._kistnae Actinomadura parvosata subsp. kistnae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TTP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TTP FirstGlance]. <br>
	</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=7ttp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ttp OCA], [https://pdbe.org/7ttp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ttp RCSB], [https://www.ebi.ac.uk/pdbsum/7ttp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ttp ProSAT]</span></td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.8Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=7ttp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ttp OCA], [https://pdbe.org/7ttp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ttp RCSB], [https://www.ebi.ac.uk/pdbsum/7ttp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ttp ProSAT]</span></td></tr>
	</table>		</table>
			== Function ==
			[https://www.uniprot.org/uniprot/A0A2P9IBF7_9ACTN A0A2P9IBF7_9ACTN]

			==See Also==
			*[[Cytochrome P450 hydroxylase 3D structures\|Cytochrome P450 hydroxylase 3D structures]]
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Actinomadura parvosata subsp. kistnae]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Cryle MJ]]		[[Category: Cryle MJ]]
	[[Category: Greule A]]		[[Category: Greule A]]
	[[Category: Izore T]]		[[Category: Izore T]]

OCA at 06:20, 12 May 2022

2022-05-12T06:20:51Z

← Older revision		Revision as of 06:20, 12 May 2022
Line 1:		Line 1:
	~~'''Unreleased structure'''~~

	~~The entry~~ 7ttp is ~~ON HOLD until Paper Publication~~		==P450 (OxyA) from kistamicin biosynthesis, mixed heme conformation==
			<StructureSection load='7ttp' size='340' side='right'caption='[[7ttp]]' scene=''>
	~~Authors~~: ~~Greule~~, A., ~~Izore~~, T., ~~Cryle~~, M.J.		== Structural highlights ==
			<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TTP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TTP FirstGlance]. <br>
	~~Description: P450 (OxyA) from kistamicin biosynthesis, mixed heme conformation~~		</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=7ttp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ttp OCA], [https://pdbe.org/7ttp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ttp RCSB], [https://www.ebi.ac.uk/pdbsum/7ttp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ttp ProSAT]</span></td></tr>
	[[Category: ~~Unreleased~~ Structures]]		</table>
	[[Category: Cryle~~, M.J~~]]		__TOC__
	[[Category: ~~Izore, T~~]]		</StructureSection>
	[[Category: ~~Greule, A~~]]		[[Category: Large Structures]]
			[[Category: Cryle MJ]]
			[[Category: Greule A]]
			[[Category: Izore T]]

OCA at 04:53, 9 March 2022

2022-03-09T04:53:24Z

← Older revision		Revision as of 04:53, 9 March 2022
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 7ttp is ON HOLD		The entry 7ttp is ON HOLD until Paper Publication

	Authors: Greule, A., Izore, T., Cryle, M.J.		Authors: Greule, A., Izore, T., Cryle, M.J.

OCA: Protected "7ttp" [edit=sysop:move=sysop]

2022-02-09T06:21:28Z

Protected "7ttp" [edit=sysop:move=sysop]

← Older revision	Revision as of 06:21, 9 February 2022
(No difference)

OCA: New page: '''Unreleased structure''' The entry 7ttp is ON HOLD Authors: Greule, A., Izore, T., Cryle, M.J. Description: P450 (OxyA) from kistamicin biosynthesis, mixed heme conformation [[Catego...

2022-02-09T06:21:27Z

New page: '''Unreleased structure''' The entry 7ttp is ON HOLD Authors: Greule, A., Izore, T., Cryle, M.J. Description: P450 (OxyA) from kistamicin biosynthesis, mixed heme conformation [[Catego...

New page

'''Unreleased structure'''

The entry 7ttp is ON HOLD

Authors: Greule, A., Izore, T., Cryle, M.J.

Description: P450 (OxyA) from kistamicin biosynthesis, mixed heme conformation
[[Category: Unreleased Structures]]
[[Category: Cryle, M.J]]
[[Category: Izore, T]]
[[Category: Greule, A]]