1csm: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1csm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CSM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CSM FirstGlance]. <br>
<table><tr><td colspan='2'>[[1csm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CSM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CSM FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene><br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Anthranilate_synthase Anthranilate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.27 4.1.3.27] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Anthranilate_synthase Anthranilate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.27 4.1.3.27] </span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1csm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1csm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1csm RCSB], [http://www.ebi.ac.uk/pdbsum/1csm PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1csm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1csm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1csm RCSB], [http://www.ebi.ac.uk/pdbsum/1csm PDBsum]</span></td></tr>
<table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Anthranilate synthase]]
[[Category: Anthranilate synthase]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Lipscomb, W N.]]
[[Category: Lipscomb, W N]]
[[Category: Xue, Y.]]
[[Category: Xue, Y]]
[[Category: Isomerase]]
[[Category: Isomerase]]

Revision as of 00:00, 23 December 2014

THE CRYSTAL STRUCTURE OF ALLOSTERIC CHORISMATE MUTASE AT 2.2 ANGSTROMS RESOLUTIONTHE CRYSTAL STRUCTURE OF ALLOSTERIC CHORISMATE MUTASE AT 2.2 ANGSTROMS RESOLUTION

Structural highlights

1csm is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:Anthranilate synthase, with EC number 4.1.3.27
Resources:FirstGlance, OCA, RCSB, PDBsum

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 PubMed

The crystal structure of an allosteric chorismate mutase, the Thr-226-->Ile mutant, from yeast Saccharomyces cerevisiae has been determined to 2.2-A resolution by using the multiple isomorphous replacement method. Solvent-flattening and electron-density modification were applied for phase improvement. The current crystallographic R factor is 0.196. The final model includes 504 of the 512 residues and 97 water molecules. In addition, two tryptophan molecules were identified in the interface between monomers. The overall structure is completely different from the reported structure of chorismate mutase from Bacillus subtilis. This structure showed 71% helices with essentially no beta-sheet structures.

The crystal structure of allosteric chorismate mutase at 2.2-A resolution.,Xue Y, Lipscomb WN, Graf R, Schnappauf G, Braus G Proc Natl Acad Sci U S A. 1994 Nov 8;91(23):10814-8. PMID:7971967[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Xue Y, Lipscomb WN, Graf R, Schnappauf G, Braus G. The crystal structure of allosteric chorismate mutase at 2.2-A resolution. Proc Natl Acad Sci U S A. 1994 Nov 8;91(23):10814-8. PMID:7971967

1csm, resolution 2.20Å

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