1dih
From Proteopedia
(New page: 200px<br /><applet load="1dih" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dih, resolution 2.2Å" /> '''THREE-DIMENSIONAL STR...) |
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| - | [[Image:1dih.gif|left|200px]]<br /><applet load="1dih" size=" | + | [[Image:1dih.gif|left|200px]]<br /><applet load="1dih" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dih, resolution 2.2Å" /> | caption="1dih, resolution 2.2Å" /> | ||
'''THREE-DIMENSIONAL STRUCTURE OF E. COLI DIHYDRODIPICOLINATE REDUCTASE'''<br /> | '''THREE-DIMENSIONAL STRUCTURE OF E. COLI DIHYDRODIPICOLINATE REDUCTASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Dihydrodipicolinate reductase is an enzyme found in bacteria and higher | + | Dihydrodipicolinate reductase is an enzyme found in bacteria and higher plants involved in the biosynthesis of diaminopimelic acid and lysine. Because these pathways are unique to bacteria and plants, they may represent attractive targets for new antimicrobial or herbicidal compounds. The three-dimensional structure of Escherichia coli dihydrodipicolinate reductase, complexed with NADPH, has been determined and refined to a crystallographic R-factor of 18.6% with diffraction data to 2.2 A resolution. The refined model contains the complete protein chain, the cofactor NADPH, and 55 water molecules. The enzyme is composed of two domains. The dinucleotide binding domain has a central seven-stranded parallel beta-sheet surrounded by four alpha-helices, with the cofactor binding site located at the carboxy-terminal edge of the sheet. The second domain contains four beta-strands and two alpha-helices that form an open mixed beta-sandwich. A possible binding site for dihydrodipicolinate has been identified in this second domain, about 12 A away from the dinucleotide binding site. This would imply that the protein must undergo some conformational change in order to perform catalysis. In the crystal, the native enzyme is a homotetramer generated by a 222 crystallographic axis. Implications of the tetrameric structure for the enzyme function are presented. Dihydrodipicolinate reductase uses both NADH and NADPH as cofactors, and analysis of its cofactor binding site allows for a molecular understanding of the enzyme's dual specificity. |
==About this Structure== | ==About this Structure== | ||
| - | 1DIH 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 NDP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Dihydrodipicolinate_reductase Dihydrodipicolinate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.26 1.3.1.26] Full crystallographic information is available from [http:// | + | 1DIH 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=NDP:'>NDP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Dihydrodipicolinate_reductase Dihydrodipicolinate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.26 1.3.1.26] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DIH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Blanchard, J | + | [[Category: Blanchard, J S.]] |
| - | [[Category: Sacchettini, J | + | [[Category: Sacchettini, J C.]] |
[[Category: Scapin, G.]] | [[Category: Scapin, G.]] | ||
[[Category: NDP]] | [[Category: NDP]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:16:53 2008'' |
Revision as of 10:16, 21 February 2008
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THREE-DIMENSIONAL STRUCTURE OF E. COLI DIHYDRODIPICOLINATE REDUCTASE
Overview
Dihydrodipicolinate reductase is an enzyme found in bacteria and higher plants involved in the biosynthesis of diaminopimelic acid and lysine. Because these pathways are unique to bacteria and plants, they may represent attractive targets for new antimicrobial or herbicidal compounds. The three-dimensional structure of Escherichia coli dihydrodipicolinate reductase, complexed with NADPH, has been determined and refined to a crystallographic R-factor of 18.6% with diffraction data to 2.2 A resolution. The refined model contains the complete protein chain, the cofactor NADPH, and 55 water molecules. The enzyme is composed of two domains. The dinucleotide binding domain has a central seven-stranded parallel beta-sheet surrounded by four alpha-helices, with the cofactor binding site located at the carboxy-terminal edge of the sheet. The second domain contains four beta-strands and two alpha-helices that form an open mixed beta-sandwich. A possible binding site for dihydrodipicolinate has been identified in this second domain, about 12 A away from the dinucleotide binding site. This would imply that the protein must undergo some conformational change in order to perform catalysis. In the crystal, the native enzyme is a homotetramer generated by a 222 crystallographic axis. Implications of the tetrameric structure for the enzyme function are presented. Dihydrodipicolinate reductase uses both NADH and NADPH as cofactors, and analysis of its cofactor binding site allows for a molecular understanding of the enzyme's dual specificity.
About this Structure
1DIH is a Single protein structure of sequence from Escherichia coli with as ligand. Active as Dihydrodipicolinate reductase, with EC number 1.3.1.26 Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase., Scapin G, Blanchard JS, Sacchettini JC, Biochemistry. 1995 Mar 21;34(11):3502-12. PMID:7893645
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