3ven: Difference between revisions

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-'''Unreleased structure'''
-The entry 3ven is ON HOLD
+==Crystal structure of the O-carbamoyltransferase TobZ==
+<StructureSection load='3ven' size='340' side='right'caption='[[3ven]], [[Resolution|resolution]] 1.57&Aring;' scene=''>
-Authors: Parthier, C., Stubbs, M.T., Goerlich, S., Jaenecke, F.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3ven]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptoalloteichus_tenebrarius Streptoalloteichus tenebrarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VEN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VEN FirstGlance]. <br>
-Description: Crystal structure of the O-carbamoyltransferase TobZ
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.57&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</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=3ven FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ven OCA], [https://pdbe.org/3ven PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ven RCSB], [https://www.ebi.ac.uk/pdbsum/3ven PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ven ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TOBZ_STRSD TOBZ_STRSD] TobZ is involved in the biosynthesis of the 2-deoxystreptamine-containing aminoglycoside antibiotics such as nebramycin 5 and 6-O-carbamoylkanamycin. Catalyzes the hydrolysis of carbamoyl phosphate and its subsequent adenylation by ATP to yield O-carbamoyladenylate. Then it catalyzes the transfer of the carbamoyl moiety from O-carbamoyladenylate to the tobramycin 6-hydroxy group to yield nebramycin 5. It catalyzes the same reaction with kanamycin A. These reactions are considerably slower in the presence of deoxy-ATP.<ref>PMID:20936279</ref> <ref>PMID:22383337</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Streptoalloteichus tenebrarius]]
+[[Category: Goerlich S]]
+[[Category: Jaenecke F]]
+[[Category: Parthier C]]
+[[Category: Stubbs MT]]