4bzx - Revision history

OCA at 12:00, 20 December 2023

OCA — Wed, 20 Dec 2023 12:00:58 GMT

←Older revision		Revision as of 12:00, 20 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4bzx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BZX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BZX FirstGlance]. <br>		<table><tr><td colspan='2'>[[4bzx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BZX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BZX FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADX:ADENOSINE-5-PHOSPHOSULFATE'>ADX</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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]] 1.7Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADX:ADENOSINE-5-PHOSPHOSULFATE'>ADX</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=4bzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bzx OCA], [https://pdbe.org/4bzx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bzx RCSB], [https://www.ebi.ac.uk/pdbsum/4bzx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bzx 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=4bzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bzx OCA], [https://pdbe.org/4bzx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bzx RCSB], [https://www.ebi.ac.uk/pdbsum/4bzx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bzx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/CYSNC_MYCTU CYSNC_MYCTU]] ATP sulfurylase may be the GTPase, regulating ATP sulfurylase activity (By similarity).[HAMAP-Rule:MF_00062] APS kinase catalyzes the synthesis of activated sulfate (By similarity).[HAMAP-Rule:MF_00062]	+	[https://www.uniprot.org/uniprot/CYSNC_MYCTU CYSNC_MYCTU] ATP sulfurylase may be the GTPase, regulating ATP sulfurylase activity (By similarity).[HAMAP-Rule:MF_00062] APS kinase catalyzes the synthesis of activated sulfate (By similarity).[HAMAP-Rule:MF_00062]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	In Mycobacterium tuberculosis the sulfate activating complex provides a key branching point in sulfate assimilation. The complex consists of two polypeptide chains, CysD and CysN. CysD is an ATP sulfurylase that, with the energy provided by the GTPase activity of CysN, forms adenosine-5'-phosphosulfate (APS) which can then enter the reductive branch of sulfate assimilation leading to the biosynthesis of cysteine. The CysN polypeptide chain also contains an APS kinase domain (CysC) that phosphorylates APS leading to 3'-phosphoadenosine-5'-phosphosulfate, the sulfate donor in the synthesis of sulfolipids. We have determined the crystal structures of CysC from M. tuberculosis as a binary complex with ADP, and as ternary complexes with ADP and APS and the ATP mimic AMP-PNP and APS, respectively, to resolutions of 1.5 A, 2.1 A and 1.7 A, respectively. CysC shows the typical APS kinase fold, and the structures provide comprehensive views of the catalytic machinery, conserved in this enzyme family. Comparison to the structure of the human homolog show highly conserved APS and ATP binding sites, questioning the feasibility of the design of specific inhibitors of mycobacterial CysC. Residue Cys556 is part of the flexible lid region that closes off the active site upon substrate binding. Mutational analysis revealed this residue as one of the determinants controlling lid closure and hence binding of the nucleotide substrate.
		+
		+	Crystal Structures of the Kinase Domain of the Sulfate-Activating Complex in Mycobacterium tuberculosis.,Poyraz O, Brunner K, Lohkamp B, Axelsson H, Hammarstrom LG, Schnell R, Schneider G PLoS One. 2015 Mar 25;10(3):e0121494. doi: 10.1371/journal.pone.0121494., eCollection 2015. PMID:25807013<ref>PMID:25807013</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4bzx" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 17:18, 7 September 2022

OCA — Wed, 07 Sep 2022 17:18:31 GMT

←Older revision		Revision as of 17:18, 7 September 2022
Line 3:		Line 3:
	<StructureSection load='4bzx' size='340' side='right'caption='[[4bzx]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='4bzx' size='340' side='right'caption='[[4bzx]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4bzx]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus~~ tuberculosis~~" (zopf 1883) klein 1884~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BZX OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4BZX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4bzx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BZX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BZX FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADX:ADENOSINE-5-PHOSPHOSULFATE'>ADX</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADX:ADENOSINE-5-PHOSPHOSULFATE'>ADX</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4bzp\|4bzp]], [[4bzq\|4bzq]]</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=4bzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bzx OCA], [https://pdbe.org/4bzx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bzx RCSB], [https://www.ebi.ac.uk/pdbsum/4bzx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bzx 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/Adenylyl-sulfate_kinase Adenylyl-sulfate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.25 2.7.1.25] </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=4bzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bzx OCA], [~~http~~://pdbe.org/4bzx PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4bzx RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4bzx PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4bzx ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CYSNC_MYCTU CYSNC_MYCTU]] ATP sulfurylase may be the GTPase, regulating ATP sulfurylase activity (By similarity).[HAMAP-Rule:MF_00062] APS kinase catalyzes the synthesis of activated sulfate (By similarity).[HAMAP-Rule:MF_00062]	+	[[https://www.uniprot.org/uniprot/CYSNC_MYCTU CYSNC_MYCTU]] ATP sulfurylase may be the GTPase, regulating ATP sulfurylase activity (By similarity).[HAMAP-Rule:MF_00062] APS kinase catalyzes the synthesis of activated sulfate (By similarity).[HAMAP-Rule:MF_00062]
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	In Mycobacterium tuberculosis the sulfate activating complex provides a key branching point in sulfate assimilation. The complex consists of two polypeptide chains, CysD and CysN. CysD is an ATP sulfurylase that, with the energy provided by the GTPase activity of CysN, forms adenosine-5'-phosphosulfate (APS) which can then enter the reductive branch of sulfate assimilation leading to the biosynthesis of cysteine. The CysN polypeptide chain also contains an APS kinase domain (CysC) that phosphorylates APS leading to 3'-phosphoadenosine-5'-phosphosulfate, the sulfate donor in the synthesis of sulfolipids. We have determined the crystal structures of CysC from M. tuberculosis as a binary complex with ADP, and as ternary complexes with ADP and APS and the ATP mimic AMP-PNP and APS, respectively, to resolutions of 1.5 A, 2.1 A and 1.7 A, respectively. CysC shows the typical APS kinase fold, and the structures provide comprehensive views of the catalytic machinery, conserved in this enzyme family. Comparison to the structure of the human homolog show highly conserved APS and ATP binding sites, questioning the feasibility of the design of specific inhibitors of mycobacterial CysC. Residue Cys556 is part of the flexible lid region that closes off the active site upon substrate binding. Mutational analysis revealed this residue as one of the determinants controlling lid closure and hence binding of the nucleotide substrate.	+
-		+
-	Crystal Structures of the Kinase Domain of the Sulfate-Activating Complex in Mycobacterium tuberculosis.,Poyraz O, Brunner K, Lohkamp B, Axelsson H, Hammarstrom LG, Schnell R, Schneider G PLoS One. 2015 Mar 25;10(3):e0121494. doi: 10.1371/journal.pone.0121494., eCollection 2015. PMID:25807013<ref>PMID:25807013</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 4bzx" style="background-color:#fffaf0;"></div>~~	+
-	~~== References ==~~	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Adenylyl-sulfate kinase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Lohkamp, B]]	+	[[Category: Mycobacterium tuberculosis]]
-	[[Category: Poyraz, O]]	+	[[Category: Lohkamp B]]
-	[[Category: Schneider, G]]	+	[[Category: Poyraz O]]
-	[[Category: Schnell, R]]	+	[[Category: Schneider G]]
-	~~[[Category: Sulfur assimilation]]~~	+	[[Category: Schnell R]]
-	~~[[Category: Transferase~~]]	+

OCA at 13:26, 13 March 2019

OCA — Wed, 13 Mar 2019 13:26:31 GMT

←Older revision		Revision as of 13:26, 13 March 2019
Line 1:		Line 1:

	==Structure of the Mycobacterium tuberculosis APS kinase CysC in complex with AMPPNP and APS==		==Structure of the Mycobacterium tuberculosis APS kinase CysC in complex with AMPPNP and APS==
-	<StructureSection load='4bzx' size='340' side='right' caption='[[4bzx]], [[Resolution\|resolution]] 1.70Å' scene=''>	+	<StructureSection load='4bzx' size='340' side='right'caption='[[4bzx]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4bzx]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BZX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BZX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4bzx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BZX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BZX FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADX:ADENOSINE-5-PHOSPHOSULFATE'>ADX</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADX:ADENOSINE-5-PHOSPHOSULFATE'>ADX</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4bzp\|4bzp]], [[4bzq\|4bzq]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4bzp\|4bzp]], [[4bzq\|4bzq]]</td></tr>
Line 25:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Adenylyl-sulfate kinase]]		[[Category: Adenylyl-sulfate kinase]]
		+	[[Category: Large Structures]]
	[[Category: Lohkamp, B]]		[[Category: Lohkamp, B]]
	[[Category: Poyraz, O]]		[[Category: Poyraz, O]]

OCA at 17:34, 18 January 2017

OCA — Wed, 18 Jan 2017 17:34:07 GMT

←Older revision		Revision as of 17:34, 18 January 2017
Line 1:		Line 1:
		+
	==Structure of the Mycobacterium tuberculosis APS kinase CysC in complex with AMPPNP and APS==		==Structure of the Mycobacterium tuberculosis APS kinase CysC in complex with AMPPNP and APS==
	<StructureSection load='4bzx' size='340' side='right' caption='[[4bzx]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='4bzx' size='340' side='right' caption='[[4bzx]], [[Resolution\|resolution]] 1.70Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4bzp\|4bzp]], [[4bzq\|4bzq]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4bzp\|4bzp]], [[4bzq\|4bzq]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenylyl-sulfate_kinase Adenylyl-sulfate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.25 2.7.1.25] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenylyl-sulfate_kinase Adenylyl-sulfate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.25 2.7.1.25] </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=4bzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bzx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bzx RCSB], [http://www.ebi.ac.uk/pdbsum/4bzx 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=4bzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bzx OCA], [http://pdbe.org/4bzx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bzx RCSB], [http://www.ebi.ac.uk/pdbsum/4bzx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bzx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	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 4bzx" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 05:46, 8 April 2015

OCA — Wed, 08 Apr 2015 05:46:22 GMT

←Older revision		Revision as of 05:46, 8 April 2015
Line 10:		Line 10:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/CYSNC_MYCTU CYSNC_MYCTU]] ATP sulfurylase may be the GTPase, regulating ATP sulfurylase activity (By similarity).[HAMAP-Rule:MF_00062] APS kinase catalyzes the synthesis of activated sulfate (By similarity).[HAMAP-Rule:MF_00062]		[[http://www.uniprot.org/uniprot/CYSNC_MYCTU CYSNC_MYCTU]] ATP sulfurylase may be the GTPase, regulating ATP sulfurylase activity (By similarity).[HAMAP-Rule:MF_00062] APS kinase catalyzes the synthesis of activated sulfate (By similarity).[HAMAP-Rule:MF_00062]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	In Mycobacterium tuberculosis the sulfate activating complex provides a key branching point in sulfate assimilation. The complex consists of two polypeptide chains, CysD and CysN. CysD is an ATP sulfurylase that, with the energy provided by the GTPase activity of CysN, forms adenosine-5'-phosphosulfate (APS) which can then enter the reductive branch of sulfate assimilation leading to the biosynthesis of cysteine. The CysN polypeptide chain also contains an APS kinase domain (CysC) that phosphorylates APS leading to 3'-phosphoadenosine-5'-phosphosulfate, the sulfate donor in the synthesis of sulfolipids. We have determined the crystal structures of CysC from M. tuberculosis as a binary complex with ADP, and as ternary complexes with ADP and APS and the ATP mimic AMP-PNP and APS, respectively, to resolutions of 1.5 A, 2.1 A and 1.7 A, respectively. CysC shows the typical APS kinase fold, and the structures provide comprehensive views of the catalytic machinery, conserved in this enzyme family. Comparison to the structure of the human homolog show highly conserved APS and ATP binding sites, questioning the feasibility of the design of specific inhibitors of mycobacterial CysC. Residue Cys556 is part of the flexible lid region that closes off the active site upon substrate binding. Mutational analysis revealed this residue as one of the determinants controlling lid closure and hence binding of the nucleotide substrate.
		+
		+	Crystal Structures of the Kinase Domain of the Sulfate-Activating Complex in Mycobacterium tuberculosis.,Poyraz O, Brunner K, Lohkamp B, Axelsson H, Hammarstrom LG, Schnell R, Schneider G PLoS One. 2015 Mar 25;10(3):e0121494. doi: 10.1371/journal.pone.0121494., eCollection 2015. PMID:25807013<ref>PMID:25807013</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 18:48, 24 December 2014

OCA — Wed, 24 Dec 2014 18:48:18 GMT

←Older revision		Revision as of 18:48, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4bzx]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BZX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BZX FirstGlance]. <br>		<table><tr><td colspan='2'>[[4bzx]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BZX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BZX FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADX:ADENOSINE-5-PHOSPHOSULFATE'>ADX</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADX:ADENOSINE-5-PHOSPHOSULFATE'>ADX</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4bzp\|4bzp]], [[4bzq\|4bzq]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4bzp\|4bzp]], [[4bzq\|4bzq]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenylyl-sulfate_kinase Adenylyl-sulfate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.25 2.7.1.25] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenylyl-sulfate_kinase Adenylyl-sulfate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.25 2.7.1.25] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4bzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bzx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bzx RCSB], [http://www.ebi.ac.uk/pdbsum/4bzx 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=4bzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bzx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bzx RCSB], [http://www.ebi.ac.uk/pdbsum/4bzx PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CYSNC_MYCTU CYSNC_MYCTU]] ATP sulfurylase may be the GTPase, regulating ATP sulfurylase activity (By similarity).[HAMAP-Rule:MF_00062] APS kinase catalyzes the synthesis of activated sulfate (By similarity).[HAMAP-Rule:MF_00062]
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Adenylyl-sulfate kinase]]		[[Category: Adenylyl-sulfate kinase]]
-	[[Category: Lohkamp, B.]]	+	[[Category: Lohkamp, B]]
-	[[Category: Poyraz, O.]]	+	[[Category: Poyraz, O]]
-	[[Category: Schneider, G.]]	+	[[Category: Schneider, G]]
-	[[Category: Schnell, R.]]	+	[[Category: Schnell, R]]
	[[Category: Sulfur assimilation]]		[[Category: Sulfur assimilation]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 09:11, 13 August 2014

OCA — Wed, 13 Aug 2014 09:11:48 GMT

←Older revision		Revision as of 09:11, 13 August 2014
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Structure of the Mycobacterium tuberculosis APS kinase CysC in complex with AMPPNP and APS==
-		+	<StructureSection load='4bzx' size='340' side='right' caption='[[4bzx]], [[Resolution\|resolution]] 1.70Å' scene=''>
-	~~The entry~~ 4bzx is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4bzx]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BZX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BZX FirstGlance]. <br>
-	~~Authors~~: ~~Poyraz~~, O., ~~Lohkamp~~, B., ~~Schnell~~, R., Schneider, G.	+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADX:ADENOSINE-5-PHOSPHOSULFATE'>ADX</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene><br>
-		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4bzp\|4bzp]], [[4bzq\|4bzq]]</td></tr>
-	~~Description~~: ~~Structure of the Mycobacterium tuberculosis APS kinase CysC in complex with AMPPNP and APS~~	+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenylyl-sulfate_kinase Adenylyl-sulfate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.25 2.7.1.25] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4bzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bzx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bzx RCSB], [http://www.ebi.ac.uk/pdbsum/4bzx PDBsum]</span></td></tr>
		+	<table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Adenylyl-sulfate kinase]]
		+	[[Category: Lohkamp, B.]]
		+	[[Category: Poyraz, O.]]
		+	[[Category: Schneider, G.]]
		+	[[Category: Schnell, R.]]
		+	[[Category: Sulfur assimilation]]
		+	[[Category: Transferase]]

OCA at 00:37, 7 August 2014

OCA — Thu, 07 Aug 2014 00:37:37 GMT

←Older revision		Revision as of 00:37, 7 August 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4bzx is ON HOLD	+	The entry 4bzx is ON HOLD until Paper Publication

	Authors: Poyraz, O., Lohkamp, B., Schnell, R., Schneider, G.		Authors: Poyraz, O., Lohkamp, B., Schnell, R., Schneider, G.

	Description: Structure of the Mycobacterium tuberculosis APS kinase CysC in complex with AMPPNP and APS		Description: Structure of the Mycobacterium tuberculosis APS kinase CysC in complex with AMPPNP and APS

OCA at 09:29, 16 July 2014

OCA — Wed, 16 Jul 2014 09:29:53 GMT

←Older revision		Revision as of 09:29, 16 July 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4bzx is ON HOLD ~~until Paper Publication~~	+	The entry 4bzx is ON HOLD

	Authors: Poyraz, O., Lohkamp, B., Schnell, R., Schneider, G.		Authors: Poyraz, O., Lohkamp, B., Schnell, R., Schneider, G.

	Description: Structure of the Mycobacterium tuberculosis APS kinase CysC in complex with AMPPNP and APS		Description: Structure of the Mycobacterium tuberculosis APS kinase CysC in complex with AMPPNP and APS

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

OCA — Wed, 07 Aug 2013 19:44:05 GMT

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

←Older revision

Revision as of 19:44, 7 August 2013