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| | <StructureSection load='4bzp' size='340' side='right'caption='[[4bzp]], [[Resolution|resolution]] 1.47Å' scene=''> | | <StructureSection load='4bzp' size='340' side='right'caption='[[4bzp]], [[Resolution|resolution]] 1.47Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4bzp]] 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=4BZP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BZP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4bzp]] 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=4BZP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BZP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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]] 1.47Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bzq|4bzq]], [[4bzx|4bzx]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=4bzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bzp OCA], [https://pdbe.org/4bzp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bzp RCSB], [https://www.ebi.ac.uk/pdbsum/4bzp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bzp ProSAT]</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=4bzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bzp OCA], [http://pdbe.org/4bzp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bzp RCSB], [http://www.ebi.ac.uk/pdbsum/4bzp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bzp 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/A5U1Y4_MYCTA A5U1Y4_MYCTA] APS kinase catalyzes the synthesis of activated sulfate.[ARBA:ARBA00002357] Catalyzes the synthesis of activated sulfate.[HAMAP-Rule:MF_00065] With CysD forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD.[HAMAP-Rule:MF_00062] |
| | <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: 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]]
| + | |
| Structural highlights
Function
A5U1Y4_MYCTA APS kinase catalyzes the synthesis of activated sulfate.[ARBA:ARBA00002357] Catalyzes the synthesis of activated sulfate.[HAMAP-Rule:MF_00065] With CysD forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD.[HAMAP-Rule:MF_00062]
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Poyraz O, Brunner K, Lohkamp B, Axelsson H, Hammarstrom LG, Schnell R, Schneider G. Crystal Structures of the Kinase Domain of the Sulfate-Activating Complex in Mycobacterium tuberculosis. PLoS One. 2015 Mar 25;10(3):e0121494. doi: 10.1371/journal.pone.0121494., eCollection 2015. PMID:25807013 doi:http://dx.doi.org/10.1371/journal.pone.0121494
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