8aln - Revision history

OCA at 08:12, 7 February 2024

OCA — Wed, 07 Feb 2024 08:12:36 GMT

←Older revision		Revision as of 08:12, 7 February 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[8aln]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_pasteurianum Clostridium pasteurianum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ALN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ALN FirstGlance]. <br>		<table><tr><td colspan='2'>[[8aln]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_pasteurianum Clostridium pasteurianum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ALN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ALN FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=402:DICARBONYL[BIS(CYANIDE-KAPPAC)]-MU-(IMINODIMETHANETHIOLATATO-1KAPPAS 2KAPPAS)-MU-(OXOMETHYLIDENE)DIIRON(2+)'>402</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></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]] 1.34Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=402:DICARBONYL[BIS(CYANIDE-KAPPAC)]-MU-(IMINODIMETHANETHIOLATATO-1KAPPAS 2KAPPAS)-MU-(OXOMETHYLIDENE)DIIRON(2+)'>402</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=8aln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8aln OCA], [https://pdbe.org/8aln PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8aln RCSB], [https://www.ebi.ac.uk/pdbsum/8aln PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8aln 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=8aln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8aln OCA], [https://pdbe.org/8aln PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8aln RCSB], [https://www.ebi.ac.uk/pdbsum/8aln PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8aln ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/PHF1_CLOPA PHF1_CLOPA]		[https://www.uniprot.org/uniprot/PHF1_CLOPA PHF1_CLOPA]
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Hydrogenases are H2 converting enzymes that harbor catalytic cofactors in which iron (Fe) ions are coordinated by biologically unusual carbon monoxide (CO) and cyanide (CN-) ligands. Extrinsic CO and CN-, however, inhibit hydrogenases. The mechanism by which CN- binds to [FeFe]-hydrogenases is not known. Here, we obtained crystal structures of the CN--treated [FeFe]-hydrogenase CpI from Clostridium pasteurianum. The high resolution of 1.39 A allowed us to distinguish intrinsic CN- and CO ligands and to show that extrinsic CN- binds to the open coordination site of the cofactor where CO is known to bind. In contrast to other inhibitors, CN- treated crystals show conformational changes of conserved residues within the proton transfer pathway which could allow a direct proton transfer between E279 and S319. This configuration has been proposed to be vital for efficient proton transfer, but has never been observed structurally.
-
-	Cyanide Binding to [FeFe]-Hydrogenase Stabilizes the Alternative Configuration of the Proton Transfer Pathway.,Duan J, Hemschemeier A, Burr DJ, Stripp ST, Hofmann E, Happe T Angew Chem Int Ed Engl. 2022 Dec 4. doi: 10.1002/anie.202216903. PMID:36464641<ref>PMID:36464641</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 8aln" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 10:08, 14 December 2022

OCA — Wed, 14 Dec 2022 10:08:25 GMT

←Older revision		Revision as of 10:08, 14 December 2022
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 8aln is ~~ON HOLD until Paper~~ Publication	+	==CO-bound [FeFe]-hydrogenase I from Clostridium pasteurianum (CpI) at 1.34 Angstrom==
		+	<StructureSection load='8aln' size='340' side='right'caption='[[8aln]], [[Resolution\|resolution]] 1.34Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[8aln]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_pasteurianum Clostridium pasteurianum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ALN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ALN FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=402:DICARBONYL[BIS(CYANIDE-KAPPAC)]-MU-(IMINODIMETHANETHIOLATATO-1KAPPAS 2KAPPAS)-MU-(OXOMETHYLIDENE)DIIRON(2+)'>402</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=8aln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8aln OCA], [https://pdbe.org/8aln PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8aln RCSB], [https://www.ebi.ac.uk/pdbsum/8aln PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8aln ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/PHF1_CLOPA PHF1_CLOPA]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Hydrogenases are H2 converting enzymes that harbor catalytic cofactors in which iron (Fe) ions are coordinated by biologically unusual carbon monoxide (CO) and cyanide (CN-) ligands. Extrinsic CO and CN-, however, inhibit hydrogenases. The mechanism by which CN- binds to [FeFe]-hydrogenases is not known. Here, we obtained crystal structures of the CN--treated [FeFe]-hydrogenase CpI from Clostridium pasteurianum. The high resolution of 1.39 A allowed us to distinguish intrinsic CN- and CO ligands and to show that extrinsic CN- binds to the open coordination site of the cofactor where CO is known to bind. In contrast to other inhibitors, CN- treated crystals show conformational changes of conserved residues within the proton transfer pathway which could allow a direct proton transfer between E279 and S319. This configuration has been proposed to be vital for efficient proton transfer, but has never been observed structurally.

-	~~Authors: Duan~~, J., ~~Hofmann~~, E., Happe, T.	+	Cyanide Binding to [FeFe]-Hydrogenase Stabilizes the Alternative Configuration of the Proton Transfer Pathway.,Duan J, Hemschemeier A, Burr DJ, Stripp ST, Hofmann E, Happe T Angew Chem Int Ed Engl. 2022 Dec 4. doi: 10.1002/anie.202216903. PMID:36464641<ref>PMID:36464641</ref>

-	~~Description: CO~~-~~bound [FeFe]~~-~~hydrogenase I from~~ Clostridium pasteurianum ~~(CpI) at 1.34 Angstrom~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
-	[[Category: Duan, J]]	+	<div class="pdbe-citations 8aln" style="background-color:#fffaf0;"></div>
-	[[Category: Happe, T]]	+	== References ==
-	[[Category: Hofmann, E]]	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Clostridium pasteurianum]]
		+	[[Category: Large Structures]]
		+	[[Category: Duan J]]
		+	[[Category: Happe T]]
		+	[[Category: Hofmann E]]

OCA at 05:34, 14 September 2022

OCA — Wed, 14 Sep 2022 05:34:32 GMT

←Older revision		Revision as of 05:34, 14 September 2022
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 8aln is ON HOLD	+	The entry 8aln is ON HOLD until Paper Publication

	Authors: Duan, J., Hofmann, E., Happe, T.		Authors: Duan, J., Hofmann, E., Happe, T.

OCA: Protected "8aln" [edit=sysop:move=sysop]

OCA — Wed, 10 Aug 2022 03:56:30 GMT

Protected "8aln" [edit=sysop:move=sysop]

←Older revision

Revision as of 03:56, 10 August 2022

OCA: New page: '''Unreleased structure''' The entry 8aln is ON HOLD Authors: Duan, J., Hofmann, E., Happe, T. Description: CO-bound [FeFe]-hydrogenase I from Clostridium pasteurianum (CpI) at 1.34 An...

OCA — Wed, 10 Aug 2022 03:56:29 GMT

New page: '''Unreleased structure''' The entry 8aln is ON HOLD Authors: Duan, J., Hofmann, E., Happe, T. Description: CO-bound [FeFe]-hydrogenase I from Clostridium pasteurianum (CpI) at 1.34 An...

New page

'''Unreleased structure'''

The entry 8aln is ON HOLD

Authors: Duan, J., Hofmann, E., Happe, T.

Description: CO-bound [FeFe]-hydrogenase I from Clostridium pasteurianum (CpI) at 1.34 Angstrom
[[Category: Unreleased Structures]]
[[Category: Duan, J]]
[[Category: Happe, T]]
[[Category: Hofmann, E]]