1pqe
From Proteopedia
| Line 5: | Line 5: | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |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] | + | |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]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1aw8|1AW8]], [[1pqf|1PQF]], [[1pqh|1PQH]], [[1ppy|1PPY]], [[1pt0|1PT0]], [[1pt1|1PT1]], [[1pyq|1PYQ]], [[1pyu|1PYU]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pqe OCA], [http://www.ebi.ac.uk/pdbsum/1pqe PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pqe RCSB]</span> | ||
}} | }} | ||
| Line 37: | Line 40: | ||
[[Category: pyruvoyl-dependent enzyme]] | [[Category: pyruvoyl-dependent enzyme]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:03:08 2008'' |
Revision as of 20:03, 30 March 2008
| |||||||
| , resolution 1.95Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | PAND (Escherichia coli) | ||||||
| Activity: | Aspartate 1-decarboxylase, with EC number 4.1.1.11 | ||||||
| Related: | 1AW8, 1PQF, 1PQH, 1PPY, 1PT0, 1PT1, 1PYQ, 1PYU
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
S25A mutant of pyruvoyl dependent aspartate decarboxylase
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
1PQE 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
Page seeded by OCA on Sun Mar 30 23:03:08 2008
Categories: Aspartate 1-decarboxylase | Escherichia coli | Single protein | Abell, C. | Blundell, T L. | Chirgadze, D Y. | Kilkenny, M L. | Lobley, C M.C. | Matak-Vinkovic, D. | Schmitzberger, F. | Smith, A G. | Vinkovic, M. | Webb, M E. | Witty, M. | Intramolecular self-processing | Pyruvoyl-dependent enzyme
