4c5m - Revision history

OCA at 12:04, 20 December 2023

OCA — Wed, 20 Dec 2023 12:04:21 GMT

←Older revision		Revision as of 12:04, 20 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c5m]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_Mu50 Staphylococcus aureus subsp. aureus Mu50]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C5M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C5M FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c5m]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_Mu50 Staphylococcus aureus subsp. aureus Mu50]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C5M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C5M FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</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]] 1.45Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</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=4c5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c5m OCA], [https://pdbe.org/4c5m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c5m RCSB], [https://www.ebi.ac.uk/pdbsum/4c5m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c5m 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=4c5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c5m OCA], [https://pdbe.org/4c5m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c5m RCSB], [https://www.ebi.ac.uk/pdbsum/4c5m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c5m ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/A0A0H3JTP0_STAAM A0A0H3JTP0_STAAM]]	+	[https://www.uniprot.org/uniprot/A0A0H3JTP0_STAAM A0A0H3JTP0_STAAM]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Pyridoxal 5'-phosphate (PLP) is the active vitamer of vitamin B6 and acts as an essential cofactor in many aspects of amino acid and sugar metabolism. The virulence and survival of pathogenic bacteria such as Mycobacterium tuberculosis depend on PLP and deficiencies in humans have also been associated with neurological disorders and inflammation. While PLP can be synthesized by a de novo pathway in bacteria and plants, most higher organisms rely on a salvage pathway that phosphorylates either pyridoxal (PL) or its related vitamers, pyridoxine (PN) and pyridoxamine (PM). PL kinases (PLKs) are essential for this phosphorylation step and are thus of major importance for cellular viability. We recently identified a pyridoxal kinase (SaPLK) as a target of the natural product antibiotic rugulactone (Ru) in Staphylococcus aureus. Surprisingly, Ru selectively modified SaPLK not at the active site cysteine, but on a remote cysteine residue. Based on structural and biochemical studies, we now provide insight into an unprecedented dual Cys charge relay network that is mandatory for PL phosphorylation. The key component is the reactive Cys 110 residue in the lid region that forms a hemithioactetal intermediate with the 4 -aldehyde of PL. This hemithioacetal, in concert with the catalytic Cys 214, increases the nucleophilicity of the PL 5 -OH group for the inline displacement reaction with the g-phosphate of ATP. A closer inspection of related enzymes reveals that Cys 110 is conserved and thus serves as a characteristic mechanistic feature for a dual-function ribokinase subfamily herein termed CC-PLKs.
		+
		+	A sub-family of bacterial ribokinases utilizes a hemithioacetal for pyridoxal phosphate salvage.,Nodwell MB, Koch MF, Alte F, Schneider S, Sieber SA J Am Chem Soc. 2014 Mar 6. PMID:24601602<ref>PMID:24601602</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4c5m" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Pyridoxal kinase\|Pyridoxal kinase]]		*[[Pyridoxal kinase\|Pyridoxal kinase]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 17:28, 7 September 2022

OCA — Wed, 07 Sep 2022 17:28:04 GMT

←Older revision		Revision as of 17:28, 7 September 2022
Line 3:		Line 3:
	<StructureSection load='4c5m' size='340' side='right'caption='[[4c5m]], [[Resolution\|resolution]] 1.45Å' scene=''>		<StructureSection load='4c5m' size='340' side='right'caption='[[4c5m]], [[Resolution\|resolution]] 1.45Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4c5m]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Staam Staam~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C5M OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4C5M FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4c5m]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_Mu50 Staphylococcus aureus subsp. aureus Mu50]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C5M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C5M FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c5j\|4c5j]], [[4c5k\|4c5k]], [[4c5l\|4c5l]], [[4c5n\|4c5n]]</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=4c5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c5m OCA], [https://pdbe.org/4c5m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c5m RCSB], [https://www.ebi.ac.uk/pdbsum/4c5m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c5m ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyridoxal_kinase Pyridoxal kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.35 2.7.1.35] </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=4c5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c5m OCA], [~~http~~://pdbe.org/4c5m PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4c5m RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4c5m PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4c5m ProSAT]</span></td></tr>	+
	</table>		</table>
-	~~<div style~~=~~"background-color:#fffaf0;">~~	+	== Function ==
-	=~~= Publication Abstract from PubMed~~ ==	+	[[https://www.uniprot.org/uniprot/A0A0H3JTP0_STAAM A0A0H3JTP0_STAAM]]
-	Pyridoxal 5'-phosphate (PLP) is the active vitamer of vitamin B6 and acts as an essential cofactor in many aspects of amino acid and sugar metabolism. The virulence and survival of pathogenic bacteria such as Mycobacterium tuberculosis depend on PLP and deficiencies in humans have also been associated with neurological disorders and inflammation. While PLP can be synthesized by a de novo pathway in bacteria and plants, most higher organisms rely on a salvage pathway that phosphorylates either pyridoxal (PL) or its related vitamers, pyridoxine (PN) and pyridoxamine (PM). PL kinases (PLKs) are essential for this phosphorylation step and are thus of major importance for cellular viability. We recently identified a pyridoxal kinase (SaPLK) as a target of the natural product antibiotic rugulactone (Ru) in Staphylococcus aureus. Surprisingly, Ru selectively modified SaPLK not at the active site cysteine, but on a remote cysteine residue. Based on structural and biochemical studies, we now provide insight into an unprecedented dual Cys charge relay network that is mandatory for PL phosphorylation. The key component is the reactive Cys 110 residue in the lid region that forms a hemithioactetal intermediate with the 4 -aldehyde of PL. This hemithioacetal, in concert with the catalytic Cys 214, increases the nucleophilicity of the PL 5 -OH group for the inline displacement reaction with the g-phosphate of ATP. A closer inspection of related enzymes reveals that Cys 110 is conserved and thus serves as a characteristic mechanistic feature for a dual-function ribokinase subfamily herein termed CC-PLKs.	+
-		+
-	~~A sub-family of bacterial ribokinases utilizes a hemithioacetal for pyridoxal phosphate salvage.,Nodwell MB, Koch MF, Alte F, Schneider S, Sieber SA J Am Chem Soc. 2014 Mar 6. PMID~~:~~24601602<ref>PMID:24601602<~~/~~ref>~~	+
-		+
-	~~From MEDLINE®~~/~~PubMed®, a database of the U~~.S. ~~National Library of Medicine.<br>~~	+
-	</~~div>~~	+
-	~~<div class="pdbe-citations 4c5m" style="background-color:#fffaf0;"><~~/~~div>~~	+

	==See Also==		==See Also==
	*[[Pyridoxal kinase\|Pyridoxal kinase]]		*[[Pyridoxal kinase\|Pyridoxal kinase]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Pyridoxal kinase]]~~	+	[[Category: Staphylococcus aureus subsp. aureus Mu50]]
-	~~[[Category: Staam~~]]	+	[[Category: Alte F]]
-	[[Category: Alte, F]]	+	[[Category: Nodwell M]]
-	[[Category: Nodwell, M]]	+	[[Category: Schneider S]]
-	[[Category: Schneider, S]]	+	[[Category: Sieber SA]]
-	[[Category: Sieber~~, S A]]~~	+
-	~~[[Category: Ribokinase]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 09:36, 20 March 2019

OCA — Wed, 20 Mar 2019 09:36:03 GMT

←Older revision		Revision as of 09:36, 20 March 2019
Line 1:		Line 1:

	==Structure of the pyridoxal kinase from Staphylococcus aureus in complex with AMP-PCP==		==Structure of the pyridoxal kinase from Staphylococcus aureus in complex with AMP-PCP==
-	<StructureSection load='4c5m' size='340' side='right' caption='[[4c5m]], [[Resolution\|resolution]] 1.45Å' scene=''>	+	<StructureSection load='4c5m' size='340' side='right'caption='[[4c5m]], [[Resolution\|resolution]] 1.45Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c5m]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Staam Staam]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C5M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C5M FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c5m]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Staam Staam]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C5M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C5M FirstGlance]. <br>
Line 25:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Pyridoxal kinase]]		[[Category: Pyridoxal kinase]]
	[[Category: Staam]]		[[Category: Staam]]

OCA at 16:29, 11 August 2016

OCA — Thu, 11 Aug 2016 16:29:27 GMT

←Older revision		Revision as of 16:29, 11 August 2016
Line 1:		Line 1:
		+
	==Structure of the pyridoxal kinase from Staphylococcus aureus in complex with AMP-PCP==		==Structure of the pyridoxal kinase from Staphylococcus aureus in complex with AMP-PCP==
	<StructureSection load='4c5m' size='340' side='right' caption='[[4c5m]], [[Resolution\|resolution]] 1.45Å' scene=''>		<StructureSection load='4c5m' size='340' side='right' caption='[[4c5m]], [[Resolution\|resolution]] 1.45Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c5j\|4c5j]], [[4c5k\|4c5k]], [[4c5l\|4c5l]], [[4c5n\|4c5n]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c5j\|4c5j]], [[4c5k\|4c5k]], [[4c5l\|4c5l]], [[4c5n\|4c5n]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyridoxal_kinase Pyridoxal kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.35 2.7.1.35] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyridoxal_kinase Pyridoxal kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.35 2.7.1.35] </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=4c5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c5m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c5m RCSB], [http://www.ebi.ac.uk/pdbsum/4c5m PDBsum]</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=4c5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c5m OCA], [http://pdbe.org/4c5m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c5m RCSB], [http://www.ebi.ac.uk/pdbsum/4c5m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c5m ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 16:		Line 17:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4c5m" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 13:07, 4 January 2015

OCA — Sun, 04 Jan 2015 13:07:27 GMT

←Older revision		Revision as of 13:07, 4 January 2015
Line 1:		Line 1:
-	~~{{STRUCTURE_4c5m\| PDB=4c5m \| SCENE= }}~~	+	==Structure of the pyridoxal kinase from Staphylococcus aureus in complex with AMP-PCP==
-	===Structure of the pyridoxal kinase from Staphylococcus aureus in complex with AMP-PCP===	+	<StructureSection load='4c5m' size='340' side='right' caption='[[4c5m]], [[Resolution\|resolution]] 1.45Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24601602}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4c5m]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Staam Staam]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C5M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C5M FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c5j\|4c5j]], [[4c5k\|4c5k]], [[4c5l\|4c5l]], [[4c5n\|4c5n]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyridoxal_kinase Pyridoxal kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.35 2.7.1.35] </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=4c5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c5m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c5m RCSB], [http://www.ebi.ac.uk/pdbsum/4c5m PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Pyridoxal 5'-phosphate (PLP) is the active vitamer of vitamin B6 and acts as an essential cofactor in many aspects of amino acid and sugar metabolism. The virulence and survival of pathogenic bacteria such as Mycobacterium tuberculosis depend on PLP and deficiencies in humans have also been associated with neurological disorders and inflammation. While PLP can be synthesized by a de novo pathway in bacteria and plants, most higher organisms rely on a salvage pathway that phosphorylates either pyridoxal (PL) or its related vitamers, pyridoxine (PN) and pyridoxamine (PM). PL kinases (PLKs) are essential for this phosphorylation step and are thus of major importance for cellular viability. We recently identified a pyridoxal kinase (SaPLK) as a target of the natural product antibiotic rugulactone (Ru) in Staphylococcus aureus. Surprisingly, Ru selectively modified SaPLK not at the active site cysteine, but on a remote cysteine residue. Based on structural and biochemical studies, we now provide insight into an unprecedented dual Cys charge relay network that is mandatory for PL phosphorylation. The key component is the reactive Cys 110 residue in the lid region that forms a hemithioactetal intermediate with the 4 -aldehyde of PL. This hemithioacetal, in concert with the catalytic Cys 214, increases the nucleophilicity of the PL 5 -OH group for the inline displacement reaction with the g-phosphate of ATP. A closer inspection of related enzymes reveals that Cys 110 is conserved and thus serves as a characteristic mechanistic feature for a dual-function ribokinase subfamily herein termed CC-PLKs.

-	~~==About this Structure==~~	+	A sub-family of bacterial ribokinases utilizes a hemithioacetal for pyridoxal phosphate salvage.,Nodwell MB, Koch MF, Alte F, Schneider S, Sieber SA J Am Chem Soc. 2014 Mar 6. PMID:24601602<ref>PMID:24601602</ref>
-	~~[[4c5m]] is~~ a ~~4 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Staam Staam]~~. ~~Full crystallographic information is available from [http~~:/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=4C5M OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group~~=~~"xtra">PMID:024601602</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+
		+	==See Also==
		+	*[[Pyridoxal kinase\|Pyridoxal kinase]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Pyridoxal kinase]]		[[Category: Pyridoxal kinase]]
	[[Category: Staam]]		[[Category: Staam]]
-	[[Category: Alte, F.]]	+	[[Category: Alte, F]]
-	[[Category: Nodwell, M.]]	+	[[Category: Nodwell, M]]
-	[[Category: Schneider, S.]]	+	[[Category: Schneider, S]]
-	[[Category: Sieber, S A.]]	+	[[Category: Sieber, S A]]
	[[Category: Ribokinase]]		[[Category: Ribokinase]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 07:46, 16 April 2014

OCA — Wed, 16 Apr 2014 07:46:42 GMT

←Older revision		Revision as of 07:46, 16 April 2014
Line 4:		Line 4:

	==About this Structure==		==About this Structure==
-	[[4c5m]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C5M OCA].	+	[[4c5m]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Staam Staam]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C5M OCA].

	==Reference==		==Reference==
	<ref group="xtra">PMID:024601602</ref><references group="xtra"/><references/>		<ref group="xtra">PMID:024601602</ref><references group="xtra"/><references/>
	[[Category: Pyridoxal kinase]]		[[Category: Pyridoxal kinase]]
		+	[[Category: Staam]]
	[[Category: Alte, F.]]		[[Category: Alte, F.]]
	[[Category: Nodwell, M.]]		[[Category: Nodwell, M.]]

OCA at 09:08, 19 March 2014

OCA — Wed, 19 Mar 2014 09:08:50 GMT

←Older revision		Revision as of 09:08, 19 March 2014
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4c5m\| PDB=4c5m \| SCENE= }}
		+	===Structure of the pyridoxal kinase from Staphylococcus aureus in complex with AMP-PCP===
		+	{{ABSTRACT_PUBMED_24601602}}

-	~~The entry~~ 4c5m is ~~ON HOLD until Paper Publication~~	+	==About this Structure==
		+	[[4c5m]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C5M OCA].

-	~~Authors~~: Nodwell, M., ~~Alte, F~~., Sieber, S.A.~~, Schneider, S.~~	+	==Reference==
-		+	<ref group="xtra">PMID:024601602</ref><references group="xtra"/><references/>
-	~~Description~~: ~~Structure of the pyridoxal kinase from Staphylococcus aureus in complex with AMP-PCP~~	+	[[Category: Pyridoxal kinase]]
		+	[[Category: Alte, F.]]
		+	[[Category: Nodwell, M.]]
		+	[[Category: Schneider, S.]]
		+	[[Category: Sieber, S A.]]
		+	[[Category: Ribokinase]]
		+	[[Category: Transferase]]

OCA: Protected "4c5m" [edit=sysop:move=sysop]

OCA — Fri, 20 Sep 2013 03:19:12 GMT

Protected "4c5m" [edit=sysop:move=sysop]

←Older revision

Revision as of 03:19, 20 September 2013

OCA: New page: '''Unreleased structure''' The entry 4c5m is ON HOLD until Paper Publication Authors: Nodwell, M., Alte, F., Sieber, S.A., Schneider, S. Description: Structure of the pyridoxal kinase ...

OCA — Fri, 20 Sep 2013 03:19:11 GMT

New page: '''Unreleased structure''' The entry 4c5m is ON HOLD until Paper Publication Authors: Nodwell, M., Alte, F., Sieber, S.A., Schneider, S. Description: Structure of the pyridoxal kinase ...

New page

'''Unreleased structure'''

The entry 4c5m is ON HOLD until Paper Publication

Authors: Nodwell, M., Alte, F., Sieber, S.A., Schneider, S.

Description: Structure of the pyridoxal kinase from Staphylococcus aureus in complex with AMP-PCP