1pt1

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|PDB= 1pt1 |SIZE=350|CAPTION= <scene name='initialview01'>1pt1</scene>, resolution 1.90&Aring;
|PDB= 1pt1 |SIZE=350|CAPTION= <scene name='initialview01'>1pt1</scene>, resolution 1.90&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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|ACTIVITY= [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]
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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>
|GENE= PAND ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
|GENE= PAND ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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|RELATEDENTRY=[[1aw8|1AW8]], [[1ppy|1PPY]], [[1pqe|1PQE]], [[1pqf|1PQF]], [[1pqh|1PQH]], [[1pt0|1PT0]], [[1pyq|1PYQ]], [[1pyu|1PYU]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pt1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pt1 OCA], [http://www.ebi.ac.uk/pdbsum/1pt1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pt1 RCSB]</span>
}}
}}
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[[Category: Webb, M E.]]
[[Category: Webb, M E.]]
[[Category: Witty, M.]]
[[Category: Witty, M.]]
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[[Category: SO4]]
 
[[Category: decarboxylase]]
[[Category: decarboxylase]]
[[Category: pantothenate pathway]]
[[Category: pantothenate pathway]]
[[Category: protein self-processing]]
[[Category: protein self-processing]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:28:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:04:09 2008''

Revision as of 20:04, 30 March 2008


PDB ID 1pt1

Drag the structure with the mouse to rotate
, resolution 1.90Å
Ligands:
Gene: PAND (Escherichia coli)
Activity: Aspartate 1-decarboxylase, with EC number 4.1.1.11
Related: 1AW8, 1PPY, 1PQE, 1PQF, 1PQH, 1PT0, 1PYQ, 1PYU


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Unprocessed Pyruvoyl Dependent Aspartate Decarboxylase with Histidine 11 Mutated to Alanine


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

1PT1 is a Single protein structure of sequence 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

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