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3ven

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==Crystal structure of the O-carbamoyltransferase TobZ==
==Crystal structure of the O-carbamoyltransferase TobZ==
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<StructureSection load='3ven' size='340' side='right' caption='[[3ven]], [[Resolution|resolution]] 1.57&Aring;' scene=''>
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<StructureSection load='3ven' size='340' side='right'caption='[[3ven]], [[Resolution|resolution]] 1.57&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ven]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptomyces_tenebrarius"_higgins_and_kastner_(1968) "streptomyces tenebrarius" higgins and kastner (1968)]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VEN FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ven]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"streptomyces_tenebrarius"_higgins_and_kastner_(1968) "streptomyces tenebrarius" higgins and kastner (1968)]. 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>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
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</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>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3veo|3veo]], [[3ver|3ver]], [[3ves|3ves]], [[3vet|3vet]], [[3vew|3vew]], [[3vex|3vex]], [[3vez|3vez]], [[3vf2|3vf2]], [[3vf4|3vf4]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3veo|3veo]], [[3ver|3ver]], [[3ves|3ves]], [[3vet|3vet]], [[3vew|3vew]], [[3vex|3vex]], [[3vez|3vez]], [[3vf2|3vf2]], [[3vf4|3vf4]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tacA, tobZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1933 "Streptomyces tenebrarius" Higgins and Kastner (1968)])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tacA, tobZ ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1933 "Streptomyces tenebrarius" Higgins and Kastner (1968)])</td></tr>
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<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=3ven FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ven OCA], [http://pdbe.org/3ven PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ven RCSB], [http://www.ebi.ac.uk/pdbsum/3ven PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ven ProSAT]</span></td></tr>
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<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>
</table>
== Function ==
== Function ==
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[[http://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>
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[[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>
<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>
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[[Category: Large Structures]]
[[Category: Goerlich, S]]
[[Category: Goerlich, S]]
[[Category: Jaenecke, F]]
[[Category: Jaenecke, F]]

Revision as of 18:41, 27 July 2022

Crystal structure of the O-carbamoyltransferase TobZ

PDB ID 3ven

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