3vf4
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| + | |||
==Crystal structure of the O-carbamoyltransferase TobZ S530A variant in complex with carbamoyl phosphate and ADP== | ==Crystal structure of the O-carbamoyltransferase TobZ S530A variant in complex with carbamoyl phosphate and ADP== | ||
<StructureSection load='3vf4' size='340' side='right' caption='[[3vf4]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='3vf4' size='340' side='right' caption='[[3vf4]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3vf4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3vf4]] 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=3VF4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VF4 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=CP:PHOSPHORIC+ACID+MONO(FORMAMIDE)ESTER'>CP</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | </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=CP:PHOSPHORIC+ACID+MONO(FORMAMIDE)ESTER'>CP</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ven|3ven]], [[3veo|3veo]], [[3ver|3ver]], [[3ves|3ves]], [[3vet|3vet]], [[3vew|3vew]], [[3vex|3vex]], [[3vez|3vez]], [[3vf2|3vf2]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ven|3ven]], [[3veo|3veo]], [[3ver|3ver]], [[3ves|3ves]], [[3vet|3vet]], [[3vew|3vew]], [[3vex|3vex]], [[3vez|3vez]], [[3vf2|3vf2]]</td></tr> | ||
| - | <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 | + | <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> |
| - | <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=3vf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vf4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vf4 RCSB], [http://www.ebi.ac.uk/pdbsum/3vf4 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=3vf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vf4 OCA], [http://pdbe.org/3vf4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vf4 RCSB], [http://www.ebi.ac.uk/pdbsum/3vf4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vf4 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[http://www.uniprot.org/uniprot/ | + | [[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> |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| 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 3vf4" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Streptoalloteichus tenebrarius]] | ||
[[Category: Goerlich, S]] | [[Category: Goerlich, S]] | ||
[[Category: Jaenecke, F]] | [[Category: Jaenecke, F]] | ||
Revision as of 14:04, 11 August 2016
Crystal structure of the O-carbamoyltransferase TobZ S530A variant in complex with carbamoyl phosphate and ADP
| |||||||||||
