1pyu

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[[Image:1pyu.jpg|left|200px]]
[[Image:1pyu.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1pyu |SIZE=350|CAPTION= <scene name='initialview01'>1pyu</scene>, resolution 1.90&Aring;
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The line below this paragraph, containing "STRUCTURE_1pyu", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_1-decarboxylase Aspartate 1-decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.11 4.1.1.11] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= PAND ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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-->
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|DOMAIN=
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{{STRUCTURE_1pyu| PDB=1pyu | SCENE= }}
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|RELATEDENTRY=[[1aw8|1aw8]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pyu OCA], [http://www.ebi.ac.uk/pdbsum/1pyu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pyu RCSB]</span>
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}}
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'''Processed Aspartate Decarboxylase Mutant with Ser25 mutated to Cys'''
'''Processed Aspartate Decarboxylase Mutant with Ser25 mutated to Cys'''
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[[Category: Webb, M E.]]
[[Category: Webb, M E.]]
[[Category: Witty, M.]]
[[Category: Witty, M.]]
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[[Category: aspartate decarboxylase]]
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[[Category: Aspartate decarboxylase]]
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[[Category: auto-processing]]
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[[Category: Auto-processing]]
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[[Category: pyruvoyl]]
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[[Category: Pyruvoyl]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:39:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:06:28 2008''
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Revision as of 02:39, 3 May 2008

Template:STRUCTURE 1pyu

Processed Aspartate Decarboxylase Mutant with Ser25 mutated to Cys


Overview

Aspartate decarboxylase, which is translated as a pro-protein, undergoes intramolecular self-cleavage at Gly24-Ser25. We have determined the crystal structures of an unprocessed native precursor, in addition to Ala24 insertion, Ala26 insertion and Gly24-->Ser, His11-->Ala, Ser25-->Ala, Ser25-->Cys and Ser25-->Thr mutants. Comparative analyses of the cleavage site reveal specific conformational constraints that govern self-processing and demonstrate that considerable rearrangement must occur. We suggest that Thr57 Ogamma and a water molecule form an 'oxyanion hole' that likely stabilizes the proposed oxyoxazolidine intermediate. Thr57 and this water molecule are probable catalytic residues able to support acid-base catalysis. The conformational freedom in the loop preceding the cleavage site appears to play a determining role in the reaction. The molecular mechanism of self-processing, presented here, emphasizes the importance of stabilization of the oxyoxazolidine intermediate. Comparison of the structural features shows significant similarity to those in other self-processing systems, and suggests that models of the cleavage site of such enzymes based on Ser-->Ala or Ser-->Thr mutants alone may lead to erroneous interpretations of the mechanism.

About this Structure

1PYU is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural constraints on protein self-processing in L-aspartate-alpha-decarboxylase., Schmitzberger F, Kilkenny ML, Lobley CM, Webb ME, Vinkovic M, Matak-Vinkovic D, Witty M, Chirgadze DY, Smith AG, Abell C, Blundell TL, EMBO J. 2003 Dec 1;22(23):6193-204. PMID:14633979 Page seeded by OCA on Sat May 3 05:39:20 2008

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