7vzn: Difference between revisions

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<table><tr><td colspan='2'>[[7vzn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_hygroscopicus Streptomyces hygroscopicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VZN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VZN FirstGlance]. <br>
<table><tr><td colspan='2'>[[7vzn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_hygroscopicus Streptomyces hygroscopicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VZN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VZN FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</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]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=83Z:(5~{S},6~{E},8~{S},9~{S},12~{R},15~{E})-21-chloranyl-12,20-dimethoxy-6,8,16-trimethyl-5,9-bis(oxidanyl)-2-azabicyclo[16.3.1]docosa-1(21),6,15,18(22),19-pentaene-3,11-dione'>83Z</scene>, <scene name='pdbligand=CA0:5-O-[(S)-(CARBAMOYLOXY)(HYDROXY)PHOSPHORYL]ADENOSINE'>CA0</scene>, <scene name='pdbligand=CP:PHOSPHORIC+ACID+MONO(FORMAMIDE)ESTER'>CP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=83Z:(5~{S},6~{E},8~{S},9~{S},12~{R},13~{E},15~{E})-21-chloranyl-12,20-dimethoxy-6,8,16-trimethyl-5,9-bis(oxidanyl)-2-azabicyclo[16.3.1]docosa-1(21),6,13,15,18(22),19-hexaene-3,11-dione'>83Z</scene>, <scene name='pdbligand=CA0:5-O-[(S)-(CARBAMOYLOXY)(HYDROXY)PHOSPHORYL]ADENOSINE'>CA0</scene>, <scene name='pdbligand=CP:PHOSPHORIC+ACID+MONO(FORMAMIDE)ESTER'>CP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=7vzn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vzn OCA], [https://pdbe.org/7vzn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vzn RCSB], [https://www.ebi.ac.uk/pdbsum/7vzn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vzn 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=7vzn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vzn OCA], [https://pdbe.org/7vzn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vzn RCSB], [https://www.ebi.ac.uk/pdbsum/7vzn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vzn ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/Q84G19_STRHY Q84G19_STRHY]  
[https://www.uniprot.org/uniprot/Q84G19_STRHY Q84G19_STRHY]  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Iterative enzymes, which catalyze sequential reactions, have the potential to improve the atom economy and diversity of industrial enzymatic processes. Redesigning one-step enzymes to be iterative biocatalysts could further enhance these processes. Carbamoyltransferases (CTases) catalyze carbamoylation, an important modification for the bioactivity of many secondary metabolites with pharmaceutical applications. To generate an iterative CTase, we determine the X-ray structure of GdmN, a one-step CTase involved in ansamycin biosynthesis. GdmN forms a face-to-face homodimer through unusual C-terminal domains, a previously unknown functional form for CTases. Structural determination of GdmN complexed with multiple intermediates elucidates the carbamoylation process and identifies key binding residues within a spacious substrate-binding pocket. Further structural and computational analyses enable multi-site enzyme engineering, resulting in an iterative CTase with the capacity for successive 7-O and 3-O carbamoylations. Our findings reveal a subclade of the CTase family and exemplify the potential of protein engineering for generating iterative enzymes.
Endowing homodimeric carbamoyltransferase GdmN with iterative functions through structural characterization and mechanistic studies.,Wei J, Zhang X, Zhou Y, Cheng X, Lin Z, Tang M, Zheng J, Wang B, Kang Q, Bai L Nat Commun. 2022 Nov 3;13(1):6617. doi: 10.1038/s41467-022-34387-2. PMID:36329057<ref>PMID:36329057</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7vzn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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__TOC__
</StructureSection>
</StructureSection>

Latest revision as of 07:44, 11 February 2026

The structure of GdmN in complex with carbamoyl adenylate intermediate and 20-O-methyl-19-chloroproansamitocin

7vzn, resolution 2.10Å

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