1mnq: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Thioesterase Domain of Picromycin Polyketide Synthase (PICS TE), pH 8.4== | ==Thioesterase Domain of Picromycin Polyketide Synthase (PICS TE), pH 8.4== | ||
<StructureSection load='1mnq' size='340' side='right' caption='[[1mnq]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1mnq' size='340' side='right'caption='[[1mnq]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1mnq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/As_4.1526 As 4.1526]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MNQ OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[1mnq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/As_4.1526 As 4.1526]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MNQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1MNQ FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kez|1kez]], [[1mn6|1mn6]], [[1mna|1mna]], [[1mo0|1mo0]]</td></tr> | </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]], [[1mo0|1mo0]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">picAIV ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=54571 AS 4.1526])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">picAIV ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=54571 AS 4.1526])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1mnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mnq OCA], [http://pdbe.org/1mnq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mnq RCSB], [http://www.ebi.ac.uk/pdbsum/1mnq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mnq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| Line 32: | Line 32: | ||
</StructureSection> | </StructureSection> | ||
[[Category: As 4 1526]] | [[Category: As 4 1526]] | ||
[[Category: Large Structures]] | |||
[[Category: Cane, D E]] | [[Category: Cane, D E]] | ||
[[Category: Khosla, C]] | [[Category: Khosla, C]] | ||
Revision as of 11:39, 2 December 2020
Thioesterase Domain of Picromycin Polyketide Synthase (PICS TE), pH 8.4Thioesterase Domain of Picromycin Polyketide Synthase (PICS TE), pH 8.4
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedModular 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
| ||||||||||||||||||