6k8w - Revision history

OCA at 10:28, 22 November 2023

2023-11-22T10:28:06Z

←Older revision		Revision as of 10:28, 22 November 2023
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	<StructureSection load='6k8w' size='340' side='right'caption='[[6k8w]], [[Resolution\|resolution]] 3.17Å' scene=''>		<StructureSection load='6k8w' size='340' side='right'caption='[[6k8w]], [[Resolution\|resolution]] 3.17Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6k8w]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K8W OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6K8W FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6k8w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Erythrobacter_dokdonensis_DSW-74 Erythrobacter dokdonensis DSW-74]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K8W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6K8W FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 3.17Å</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=6k8w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k8w OCA], [~~http~~://pdbe.org/6k8w PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6k8w RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6k8w PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6k8w ProSAT]</span></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6k8w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k8w OCA], [https://pdbe.org/6k8w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6k8w RCSB], [https://www.ebi.ac.uk/pdbsum/6k8w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6k8w ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/A0A1A7BFR5_9SPHN A0A1A7BFR5_9SPHN]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Erythrobacter dokdonensis DSW-74]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Kim, K J]]	+	[[Category: Kim K-J]]
-	[[Category: Kim, S]]	+	[[Category: Kim S]]
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Sdr domain~~]]	+

OCA at 09:39, 18 March 2020

2020-03-18T09:39:20Z

←Older revision		Revision as of 09:39, 18 March 2020
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-	'''Unreleased structure'''

-	~~The entry~~ 6k8w is ~~ON HOLD until Paper~~ Publication	+	==Crystal structure of N-domain with NADP of baterial malonyl-CoA reductase==
		+	<StructureSection load='6k8w' size='340' side='right'caption='[[6k8w]], [[Resolution\|resolution]] 3.17Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[6k8w]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K8W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6K8W FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6k8w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k8w OCA], [http://pdbe.org/6k8w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k8w RCSB], [http://www.ebi.ac.uk/pdbsum/6k8w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k8w ProSAT]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The bi-functional malonyl-CoA reductase is a key enzyme of the 3-hydroxypropionate bi-cycle for bacterial CO2 fixation, catalysing the reduction of malonyl-CoA to malonate semialdehyde and further reduction to 3-hydroxypropionate. Here, we report the crystal structure and the full-length architecture of malonyl-CoA reductase from Porphyrobacter dokdonensis. The malonyl-CoA reductase monomer of 1230 amino acids consists of four tandemly arranged short-chain dehydrogenases/reductases, with two catalytic and two non-catalytic short-chain dehydrogenases/reductases, and forms a homodimer through paring contact of two malonyl-CoA reductase monomers. The complex structures with its cofactors and substrates revealed that the malonyl-CoA substrate site is formed by the cooperation of two short-chain dehydrogenases/reductases and one novel extra domain, while only one catalytic short-chain dehydrogenase/reductase contributes to the formation of the malonic semialdehyde-binding site. The phylogenetic and structural analyses also suggest that the bacterial bi-functional malonyl-CoA has a structural origin that is completely different from the archaeal mono-functional malonyl-CoA and malonic semialdehyde reductase, and thereby constitute an efficient enzyme.

-	~~Authors:~~ Kim, S., Kim~~, K~~.-J.	+	Structural insight into bi-functional malonyl-CoA reductase.,Son HF, Kim S, Seo H, Hong J, Lee D, Jin KS, Park S, Kim KJ Environ Microbiol. 2020 Feb;22(2):752-765. doi: 10.1111/1462-2920.14885. Epub, 2019 Dec 20. PMID:31814251<ref>PMID:31814251</ref>

-	~~Description: Crystal structure~~ of ~~N-domain with NADP~~ of ~~baterial malonyl~~-~~CoA reductase~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
		+	<div class="pdbe-citations 6k8w" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Kim, K J]]
	[[Category: Kim, S]]		[[Category: Kim, S]]
-	[[Category: ~~Kim, K.-J~~]]	+	[[Category: Oxidoreductase]]
		+	[[Category: Sdr domain]]

OCA at 04:03, 3 July 2019

2019-07-03T04:03:17Z

←Older revision		Revision as of 04:03, 3 July 2019
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6k8w is ON HOLD	+	The entry 6k8w is ON HOLD until Paper Publication

	Authors: Kim, S., Kim, K.-J.		Authors: Kim, S., Kim, K.-J.

OCA: Protected "6k8w" [edit=sysop:move=sysop]

2019-06-19T04:08:05Z

Protected "6k8w" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:08, 19 June 2019

OCA: New page: '''Unreleased structure''' The entry 6k8w is ON HOLD Authors: Kim, S., Kim, K.-J. Description: Crystal structure of N-domain with NADP of baterial malonyl-CoA reductase [[Category: Unr...

2019-06-19T04:08:03Z

New page: '''Unreleased structure''' The entry 6k8w is ON HOLD Authors: Kim, S., Kim, K.-J. Description: Crystal structure of N-domain with NADP of baterial malonyl-CoA reductase [[Category: Unr...

New page

'''Unreleased structure'''

The entry 6k8w is ON HOLD

Authors: Kim, S., Kim, K.-J.

Description: Crystal structure of N-domain with NADP of baterial malonyl-CoA reductase
[[Category: Unreleased Structures]]
[[Category: Kim, S]]
[[Category: Kim, K.-J]]