1u80
From Proteopedia
(New page: 200px<br /><applet load="1u80" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u80, resolution 2.85Å" /> '''Phosphopantothenoylc...) |
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| - | [[Image:1u80.gif|left|200px]]<br /><applet load="1u80" size=" | + | [[Image:1u80.gif|left|200px]]<br /><applet load="1u80" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1u80, resolution 2.85Å" /> | caption="1u80, resolution 2.85Å" /> | ||
'''Phosphopantothenoylcysteine synthetase from E. coli, CMP complex'''<br /> | '''Phosphopantothenoylcysteine synthetase from E. coli, CMP complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Phosphopantothenoylcysteine (PPC) synthetase forms a peptide bond between | + | Phosphopantothenoylcysteine (PPC) synthetase forms a peptide bond between 4'-phosphopantothenate and cysteine in coenzyme A biosynthesis. PPC synthetases fall into two classes: eukaryotic, ATP-dependent and eubacterial, CTP-dependent enzymes. We describe the first crystal structure of E. coli PPC synthetase as a prototype of bacterial, CTP-dependent PPC synthetases. Structures of the apo-form and the synthetase complexed with CTP, the activated acyl-intermediate, 4'-phosphopantothenoyl-CMP, and with the reaction product CMP provide snapshots along the reaction pathway and detailed insight into substrate binding and the reaction mechanism of peptide bond formation. Binding of the phosphopantothenate moiety of the acyl-intermediate in a cleft at the C-terminal end of the central beta sheet of the dinucleotide binding fold is accomplished by an otherwise flexible flap. A second disordered loop may control access of cysteine to the active site. The conservation of functionalities involved in substrate binding and catalysis provides insight into similarities and differences of prokaryotic and eukaryotic PPC synthetases. |
==About this Structure== | ==About this Structure== | ||
| - | 1U80 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PO4 and C5P as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphopantothenate--cysteine_ligase Phosphopantothenate--cysteine ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.5 6.3.2.5] Full crystallographic information is available from [http:// | + | 1U80 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=C5P:'>C5P</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphopantothenate--cysteine_ligase Phosphopantothenate--cysteine ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.5 6.3.2.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U80 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Phosphopantothenate--cysteine ligase]] | [[Category: Phosphopantothenate--cysteine ligase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Augustin, M | + | [[Category: Augustin, M A.]] |
[[Category: Huber, R.]] | [[Category: Huber, R.]] | ||
[[Category: Kupke, T.]] | [[Category: Kupke, T.]] | ||
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[[Category: coenzyme a biosynthesis]] | [[Category: coenzyme a biosynthesis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:21:35 2008'' |
Revision as of 13:21, 21 February 2008
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Phosphopantothenoylcysteine synthetase from E. coli, CMP complex
Overview
Phosphopantothenoylcysteine (PPC) synthetase forms a peptide bond between 4'-phosphopantothenate and cysteine in coenzyme A biosynthesis. PPC synthetases fall into two classes: eukaryotic, ATP-dependent and eubacterial, CTP-dependent enzymes. We describe the first crystal structure of E. coli PPC synthetase as a prototype of bacterial, CTP-dependent PPC synthetases. Structures of the apo-form and the synthetase complexed with CTP, the activated acyl-intermediate, 4'-phosphopantothenoyl-CMP, and with the reaction product CMP provide snapshots along the reaction pathway and detailed insight into substrate binding and the reaction mechanism of peptide bond formation. Binding of the phosphopantothenate moiety of the acyl-intermediate in a cleft at the C-terminal end of the central beta sheet of the dinucleotide binding fold is accomplished by an otherwise flexible flap. A second disordered loop may control access of cysteine to the active site. The conservation of functionalities involved in substrate binding and catalysis provides insight into similarities and differences of prokaryotic and eukaryotic PPC synthetases.
About this Structure
1U80 is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as Phosphopantothenate--cysteine ligase, with EC number 6.3.2.5 Full crystallographic information is available from OCA.
Reference
Structural basis of CTP-dependent peptide bond formation in coenzyme A biosynthesis catalyzed by Escherichia coli PPC synthetase., Stanitzek S, Augustin MA, Huber R, Kupke T, Steinbacher S, Structure. 2004 Nov;12(11):1977-88. PMID:15530362
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