1ppy: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1ppy |SIZE=350|CAPTION= <scene name='initialview01'>1ppy</scene>, resolution 1.95Å | |PDB= 1ppy |SIZE=350|CAPTION= <scene name='initialview01'>1ppy</scene>, resolution 1.95Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |LIGAND= <scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|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 OR B0131 OR C0160 OR Z0142 OR ECS0135 OR SF0128 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= PAND OR B0131 OR C0160 OR Z0142 OR ECS0135 OR SF0128 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1aw8|1aw8]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ppy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ppy OCA], [http://www.ebi.ac.uk/pdbsum/1ppy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ppy RCSB]</span> | |||
}} | }} | ||
| Line 34: | Line 37: | ||
[[Category: Webb, M E.]] | [[Category: Webb, M E.]] | ||
[[Category: Witty, M.]] | [[Category: Witty, M.]] | ||
[[Category: decarboxylase]] | [[Category: decarboxylase]] | ||
[[Category: intramolecular protein self-processing]] | [[Category: intramolecular protein self-processing]] | ||
[[Category: pantothenate pathway]] | [[Category: pantothenate pathway]] | ||
''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 23:02:59 2008'' | ||
Revision as of 23:03, 30 March 2008
| |||||||
| , resolution 1.95Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | PAND OR B0131 OR C0160 OR Z0142 OR ECS0135 OR SF0128 (Escherichia coli) | ||||||
| Activity: | Aspartate 1-decarboxylase, with EC number 4.1.1.11 | ||||||
| Related: | 1aw8
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Native precursor of pyruvoyl dependent Aspartate decarboxylase
OverviewOverview
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 StructureAbout this Structure
1PPY is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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 23:02:59 2008