1mo2: Difference between revisions

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New page: left|200px<br /><applet load="1mo2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mo2, resolution 3.00Å" /> '''Thioesterase Domain ...
 
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[[Image:1mo2.jpg|left|200px]]<br /><applet load="1mo2" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1mo2, resolution 3.00&Aring;" />
'''Thioesterase Domain from 6-Deoxyerythronolide Synthase (DEBS TE), pH 8.5'''<br />


==Overview==
==Thioesterase Domain from 6-Deoxyerythronolide Synthase (DEBS TE), pH 8.5==
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.
<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/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='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='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]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mo/1mo2_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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>


==About this Structure==
==See Also==
1MO2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharopolyspora_erythraea Saccharopolyspora erythraea]. Active as [http://en.wikipedia.org/wiki/Erythronolide_synthase Erythronolide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.94 2.3.1.94] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MO2 OCA].
*[[6-deoxyerythronolide B synthase (DEBS)|6-deoxyerythronolide B synthase (DEBS)]]
 
*[[6-deoxyerythronolide B synthase 3D structures|6-deoxyerythronolide B synthase 3D structures]]
==Reference==
__TOC__
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12379102 12379102]
</StructureSection>
[[Category: Erythronolide synthase]]
[[Category: Large Structures]]
[[Category: Saccharopolyspora erythraea]]
[[Category: Saccharopolyspora erythraea]]
[[Category: Single protein]]
[[Category: Cane DE]]
[[Category: Cane, D.E.]]
[[Category: Khosla C]]
[[Category: Khosla, C.]]
[[Category: Lu H]]
[[Category: Lu, H.]]
[[Category: Stroud RM]]
[[Category: Stroud, R.M.]]
[[Category: Tsai S-C]]
[[Category: Tsai, S.C.]]
[[Category: 6-deoxyerythronolide]]
[[Category: alpha beta hydrolase]]
[[Category: erythromycin]]
[[Category: open substrate channel]]
[[Category: picromycin]]
[[Category: pikromycin]]
[[Category: pks]]
[[Category: polyketide synthase]]
[[Category: te]]
[[Category: thioesterase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:34:21 2007''

Latest revision as of 07:46, 14 February 2024

Thioesterase Domain from 6-Deoxyerythronolide Synthase (DEBS TE), pH 8.5

1mo2, resolution 3.00Å

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