1e3a: Difference between revisions
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[[Image:1e3a.gif|left|200px]] | [[Image:1e3a.gif|left|200px]] | ||
'''A SLOW PROCESSING PRECURSOR PENICILLIN ACYLASE FROM ESCHERICHIA COLI''' | {{Structure | ||
|PDB= 1e3a |SIZE=350|CAPTION= <scene name='initialview01'>1e3a</scene>, resolution 1.8Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Penicillin_amidase Penicillin amidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.11 3.5.1.11] | |||
|GENE= PAC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''A SLOW PROCESSING PRECURSOR PENICILLIN ACYLASE FROM ESCHERICHIA COLI''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1E3A is a [ | 1E3A is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E3A OCA]. | ||
==Reference== | ==Reference== | ||
Structure of a slow processing precursor penicillin acylase from Escherichia coli reveals the linker peptide blocking the active-site cleft., Hewitt L, Kasche V, Lummer K, Lewis RJ, Murshudov GN, Verma CS, Dodson GG, Wilson KS, J Mol Biol. 2000 Sep 29;302(4):887-98. PMID:[http:// | Structure of a slow processing precursor penicillin acylase from Escherichia coli reveals the linker peptide blocking the active-site cleft., Hewitt L, Kasche V, Lummer K, Lewis RJ, Murshudov GN, Verma CS, Dodson GG, Wilson KS, J Mol Biol. 2000 Sep 29;302(4):887-98. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10993730 10993730] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Penicillin amidase]] | [[Category: Penicillin amidase]] | ||
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[[Category: ntn-hydrolase]] | [[Category: ntn-hydrolase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:48:52 2008'' | ||
Revision as of 11:48, 20 March 2008
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| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | PAC (Escherichia coli) | ||||||
| Activity: | Penicillin amidase, with EC number 3.5.1.11 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
A SLOW PROCESSING PRECURSOR PENICILLIN ACYLASE FROM ESCHERICHIA COLI
OverviewOverview
Penicillin G acylase is a periplasmic protein, cytoplasmically expressed as a precursor polypeptide comprising a signal sequence, the A and B chains of the mature enzyme (209 and 557 residues respectively) joined by a spacer peptide of 54 amino acid residues. The wild-type AB heterodimer is produced by proteolytic removal of this spacer in the periplasm. The first step in processing is believed to be autocatalytic hydrolysis of the peptide bond between the C-terminal residue of the spacer and the active-site serine residue at the N terminus of the B chain. We have determined the crystal structure of a slowly processing precursor mutant (Thr263Gly) of penicillin G acylase from Escherichia coli, which reveals that the spacer peptide blocks the entrance to the active-site cleft consistent with an autocatalytic mechanism of maturation. In this mutant precursor there is, however, an unexpected cleavage at a site four residues from the active-site serine residue. Analyses of the stereochemistry of the 260-261 bond seen to be cleaved in this precursor structure and of the 263-264 peptide bond have suggested factors that may govern the autocatalytic mechanism.
About this StructureAbout this Structure
1E3A is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Structure of a slow processing precursor penicillin acylase from Escherichia coli reveals the linker peptide blocking the active-site cleft., Hewitt L, Kasche V, Lummer K, Lewis RJ, Murshudov GN, Verma CS, Dodson GG, Wilson KS, J Mol Biol. 2000 Sep 29;302(4):887-98. PMID:10993730
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