1tuw
From Proteopedia
(Difference between revisions)
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<StructureSection load='1tuw' size='340' side='right'caption='[[1tuw]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1tuw' size='340' side='right'caption='[[1tuw]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1tuw]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1tuw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_glaucescens Streptomyces glaucescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TUW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TUW FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tuw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tuw OCA], [https://pdbe.org/1tuw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tuw RCSB], [https://www.ebi.ac.uk/pdbsum/1tuw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tuw ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/TCMI_STRGA TCMI_STRGA] Required for conversion of tetracenomycin F2 to tetracenomycin D3. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1tuw ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1tuw ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Tetracenomycin F2 cyclase (tcmI gene product), catalyzes an aromatic rearrangement in the biosynthetic pathway for tetracenomycin C in Streptomyces glaucescens. The x-ray structure of this small enzyme has been determined to 1.9-A resolution together with an analysis of site-directed mutants of potential catalytic residues. The protein exhibits a dimeric betaalphabeta ferredoxin-like fold that utilizes strand swapping between subunits in its assembly. The fold is dominated by four strands of antiparallel sheet and a layer of alpha-helices, which creates a cavity that is proposed to be the active site. This type of secondary structural arrangement has been previously observed in polyketide monooxygenases and suggests an evolutionary relationship between enzymes that catalyze adjacent steps in these biosynthetic pathways. Mutational analysis of all of the obvious catalytic bases within the active site suggests that the enzyme functions to steer the chemical outcome of the cyclization rather than providing a specific catalytic group. Together, the structure and functional analysis provide insight into the structural framework necessary to perform the complex rearrangements catalyzed by this class of polyketide cyclases. | ||
- | |||
- | Structural and functional analysis of tetracenomycin F2 cyclase from Streptomyces glaucescens. A type II polyketide cyclase.,Thompson TB, Katayama K, Watanabe K, Hutchinson CR, Rayment I J Biol Chem. 2004 Sep 3;279(36):37956-63. Epub 2004 Jun 30. PMID:15231835<ref>PMID:15231835</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1tuw" style="background-color:#fffaf0;"></div> | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Actinomyces glaucescens preobrazhenskaya in gauze et al. 1957]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Hutchinson | + | [[Category: Streptomyces glaucescens]] |
- | [[Category: Katayama | + | [[Category: Hutchinson CR]] |
- | [[Category: Rayment | + | [[Category: Katayama K]] |
- | [[Category: Thompson | + | [[Category: Rayment I]] |
- | [[Category: Watanabe | + | [[Category: Thompson TB]] |
- | + | [[Category: Watanabe K]] | |
- | + |
Current revision
Structural and Functional Analysis of Tetracenomycin F2 Cyclase from Streptomyces glaucescens: A Type-II Polyketide Cyclase
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