This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1p9o
From Proteopedia
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | The structure of human phosphopantothenoylcysteine (PPC) synthetase was | + | The structure of human phosphopantothenoylcysteine (PPC) synthetase was determined at 2.3 A resolution. PPC synthetase is a dimer with identical monomers. Some features of the monomer fold resemble a group of NAD-dependent enzymes, while other features resemble the ribokinase fold. The ATP, phosphopantothenate, and cysteine binding sites were deduced from modeling studies. Highly conserved ATP binding residues include Gly43, Ser61, Gly63, Gly66, Phe230, and Asn258. Highly conserved phosphopantothenate binding residues include Asn59, Ala179, Ala180, and Asp183 from one monomer and Arg55' from the adjacent monomer. The structure predicts a ping pong mechanism with initial formation of an acyladenylate intermediate, followed by release of pyrophosphate and attack by cysteine to form the final products PPC and AMP. |
==About this Structure== | ==About this Structure== | ||
| Line 14: | Line 14: | ||
[[Category: Phosphopantothenate--cysteine ligase]] | [[Category: Phosphopantothenate--cysteine ligase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Begley, T | + | [[Category: Begley, T P.]] |
| - | [[Category: Ealick, S | + | [[Category: Ealick, S E.]] |
[[Category: Manoj, N.]] | [[Category: Manoj, N.]] | ||
[[Category: Strauss, E.]] | [[Category: Strauss, E.]] | ||
| Line 21: | Line 21: | ||
[[Category: synthetase]] | [[Category: synthetase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:26:47 2008'' |
Revision as of 12:26, 21 February 2008
|
Crystal Structure of Phosphopantothenoylcysteine Synthetase
Overview
The structure of human phosphopantothenoylcysteine (PPC) synthetase was determined at 2.3 A resolution. PPC synthetase is a dimer with identical monomers. Some features of the monomer fold resemble a group of NAD-dependent enzymes, while other features resemble the ribokinase fold. The ATP, phosphopantothenate, and cysteine binding sites were deduced from modeling studies. Highly conserved ATP binding residues include Gly43, Ser61, Gly63, Gly66, Phe230, and Asn258. Highly conserved phosphopantothenate binding residues include Asn59, Ala179, Ala180, and Asp183 from one monomer and Arg55' from the adjacent monomer. The structure predicts a ping pong mechanism with initial formation of an acyladenylate intermediate, followed by release of pyrophosphate and attack by cysteine to form the final products PPC and AMP.
About this Structure
1P9O is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Phosphopantothenate--cysteine ligase, with EC number 6.3.2.5 Full crystallographic information is available from OCA.
Reference
Structure of human phosphopantothenoylcysteine synthetase at 2.3 A resolution., Manoj N, Strauss E, Begley TP, Ealick SE, Structure. 2003 Aug;11(8):927-36. PMID:12906824
Page seeded by OCA on Thu Feb 21 14:26:47 2008
