1mo2: Difference between revisions

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 <StructureSection load='1mo2' size='340' side='right'caption='[[1mo2]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mo2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"actinomyces_erythreus"_(sic)_waksman_1923 "actinomyces erythreus" (sic) waksman 1923]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MO2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MO2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mo2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharopolyspora_erythraea Saccharopolyspora erythraea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MO2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MO2 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1kez|1kez]], [[1mn6|1mn6]], [[1mna|1mna]], [[1mnq|1mnq]]</div></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]] 3&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ERYA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1836 "Actinomyces erythreus" (sic) Waksman 1923])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/6-deoxyerythronolide-B_synthase 6-deoxyerythronolide-B synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.94 2.3.1.94] </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=1mo2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mo2 OCA], [https://pdbe.org/1mo2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mo2 RCSB], [https://www.ebi.ac.uk/pdbsum/1mo2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mo2 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/ERYA3_SACER ERYA3_SACER]
 == Evolutionary Conservation ==
 [[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=1mo2 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Modular polyketide synthases (PKSs) synthesize the polyketide cores of pharmacologically important natural products such as erythromycin and picromycin. Understanding PKSs at high resolution could present new opportunities for chemoenzymatic synthesis of complex molecules. The crystal structures of macrocycle-forming thioesterase (TE) domains from the picromycin synthase (PICS) and 6-deoxyerythronolide B synthase (DEBS) were determined to 1.8-3.0 A with an R(crys) of 19.2-24.4%, including three structures of PICS TE (crystallized at pH 7.6, 8.0, and 8.4) and a second crystal form of DEBS TE. As predicted by the previous work on DEBS TE [Tsai, S. C., et al. (2001) Proc. Natl. Acad. Sci. U.S.A. 98, 14808-14813], PICS TE contains an open substrate channel and a hydrophobic dimer interface. Notwithstanding their similarity, the dimer interfaces and substrate channels of DEBS TE and PICS TE reveal key differences. The structural basis for the divergent substrate specificities of DEBS TE and PICS TE is analyzed. The size of the substrate channel increases with increasing pH, presumably due to electrostatic repulsion in the channel at elevated pH. Together, these structures support previous predictions that macrocycle-forming thioesterases from PKSs share the same protein fold, an open substrate channel, a similar catalytic mechanism, and a hydrophobic dimer interface. They also provide a basis for the design of enzymes capable of catalyzing regioselective macrocyclization of natural or synthetic substrates. A series of high-resolution snapshots of a protein channel at different pHs is presented alongside analysis of channel residues, which could help in the redesign of the protein channel architecture.
-Insights into channel architecture and substrate specificity from crystal structures of two macrocycle-forming thioesterases of modular polyketide synthases.,Tsai SC, Lu H, Cane DE, Khosla C, Stroud RM Biochemistry. 2002 Oct 22;41(42):12598-606. PMID:12379102<ref>PMID:12379102</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1mo2" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[6-deoxyerythronolide B synthase (DEBS)|6-deoxyerythronolide B synthase (DEBS)]]
 *[[6-deoxyerythronolide B synthase 3D structures|6-deoxyerythronolide B synthase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: 6-deoxyerythronolide-B synthase]]
 [[Category: Large Structures]]
-[[Category: Cane, D E]]
+[[Category: Saccharopolyspora erythraea]]
-[[Category: Khosla, C]]
+[[Category: Cane DE]]
-[[Category: Lu, H]]
+[[Category: Khosla C]]
-[[Category: Stroud, R M]]
+[[Category: Lu H]]
-[[Category: Tsai, S C]]
+[[Category: Stroud RM]]
-[[Category: 6-deoxyerythronolide]]
+[[Category: Tsai S-C]]
-[[Category: Alpha beta hydrolase]]
-[[Category: Erythromycin]]
-[[Category: Open substrate channel]]
-[[Category: Picromycin]]
-[[Category: Pikromycin]]
-[[Category: Pk]]
-[[Category: Polyketide synthase]]
-[[Category: Te]]
-[[Category: Thioesterase]]
-[[Category: Transferase]]