1mli
From Proteopedia
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==CRYSTAL STRUCTURE OF MUCONOLACTONE ISOMERASE AT 3.3 ANGSTROMS RESOLUTION== | ==CRYSTAL STRUCTURE OF MUCONOLACTONE ISOMERASE AT 3.3 ANGSTROMS RESOLUTION== | ||
- | <StructureSection load='1mli' size='340' side='right' caption='[[1mli]], [[Resolution|resolution]] 3.30Å' scene=''> | + | <StructureSection load='1mli' size='340' side='right'caption='[[1mli]], [[Resolution|resolution]] 3.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1mli]] is a 10 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1mli]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MLI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MLI 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]] 3.3Å</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=1mli FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mli OCA], [https://pdbe.org/1mli PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mli RCSB], [https://www.ebi.ac.uk/pdbsum/1mli PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mli ProSAT]</span></td></tr> |
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/CATC_PSEPU CATC_PSEPU] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
- | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ml/1mli_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ml/1mli_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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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=1mli 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=1mli ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The crystal structure of muconolactone isomerase from Pseudomonas putida, a unique molecule with ten 96 amino acid subunits and 5-fold, and 2-fold symmetries, has been solved at 3.3 A resolution. The non-crystallographic symmetries were used to refine the initial single isomorphous replacement phases and produce an interpretable 10-fold averaged map. The backbone trace is complete and confirmed by the amino acid sequence fit. Each subunit is composed of a body with two alpha-helices and an antiparallel twisted beta-sheet of four strands, and an extended arm. The helices and the sheet fold to form a two-layered structure with an enclosed hydrophobic core and a partially formed putative active site pocket. The C-terminal arm of another subunit related by a local dyad symmetry extends over the core to complete this pocket. The decameric protein is almost spherical, with the helices forming the external coat. There is a large hydrophilic cavity in the center with open ends along the 5-fold axis. Molecular interactions between subunits are extensive. Each subunit contacts four neighbors and loses nearly 40% of its solvent contact area on oligomerization. | ||
- | |||
- | Crystal structure of muconolactone isomerase at 3.3 A resolution.,Katti SK, Katz BA, Wyckoff HW J Mol Biol. 1989 Feb 5;205(3):557-71. PMID:2926818<ref>PMID:2926818</ref> | ||
- | |||
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1mli" style="background-color:#fffaf0;"></div> | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: | + | [[Category: Pseudomonas putida]] |
- | [[Category: Katti | + | [[Category: Katti SK]] |
- | [[Category: Katz | + | [[Category: Katz BA]] |
- | [[Category: Wyckoff | + | [[Category: Wyckoff HW]] |
- | + |
Current revision
CRYSTAL STRUCTURE OF MUCONOLACTONE ISOMERASE AT 3.3 ANGSTROMS RESOLUTION
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