1twi
From Proteopedia
(New page: 200px<br /><applet load="1twi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1twi, resolution 2.00Å" /> '''Crystal structure of...) |
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| - | [[Image:1twi.gif|left|200px]]<br /><applet load="1twi" size=" | + | [[Image:1twi.gif|left|200px]]<br /><applet load="1twi" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1twi, resolution 2.00Å" /> | caption="1twi, resolution 2.00Å" /> | ||
'''Crystal structure of Diaminopimelate Decarboxylase from m. jannaschii in co-complex with L-lysine'''<br /> | '''Crystal structure of Diaminopimelate Decarboxylase from m. jannaschii in co-complex with L-lysine'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cocrystal structures of Methanococcus jannaschii diaminopimelate | + | Cocrystal structures of Methanococcus jannaschii diaminopimelate decarboxylase (DAPDC) bound to a substrate analog, azelaic acid, and its L-lysine product have been determined at 2.6 A and 2.0 A, respectively. This PLP-dependent enzyme is responsible for the final step of L-lysine biosynthesis in bacteria and plays a role in beta-lactam antibiotic resistance in Staphylococcus aureus. Substrate specificity derives from recognition of the L-chiral center of diaminopimelate and a system of ionic "molecular rulers" that dictate substrate length. A coupled-enzyme assay system permitted measurement of kinetic parameters for recombinant DAPDCs and inhibition constants (K(i)) for azelaic acid (89 microM) and other substrate analogs. Implications for rational design of broad-spectrum antimicrobial agents targeted against DAPDCs of drug-resistant strains of bacterial pathogens, such as Staphylococcus aureus, are discussed. |
==About this Structure== | ==About this Structure== | ||
| - | 1TWI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with MG, LYS and PLP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Diaminopimelate_decarboxylase Diaminopimelate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.20 4.1.1.20] Full crystallographic information is available from [http:// | + | 1TWI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=LYS:'>LYS</scene> and <scene name='pdbligand=PLP:'>PLP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Diaminopimelate_decarboxylase Diaminopimelate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.20 4.1.1.20] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TWI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Methanocaldococcus jannaschii]] | [[Category: Methanocaldococcus jannaschii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bonanno, J | + | [[Category: Bonanno, J B.]] |
| - | [[Category: Burley, S | + | [[Category: Burley, S K.]] |
[[Category: He, G.]] | [[Category: He, G.]] | ||
| - | [[Category: Lencastre, H | + | [[Category: Lencastre, H De.]] |
| - | [[Category: NYSGXRC, New | + | [[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]] |
| - | [[Category: Pinho, M | + | [[Category: Pinho, M G.]] |
| - | [[Category: Rajashankar, K | + | [[Category: Rajashankar, K R.]] |
| - | [[Category: Ray, S | + | [[Category: Ray, S S.]] |
[[Category: Tomasz, A.]] | [[Category: Tomasz, A.]] | ||
[[Category: LYS]] | [[Category: LYS]] | ||
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[[Category: t135]] | [[Category: t135]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:18:05 2008'' |
Revision as of 13:18, 21 February 2008
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Crystal structure of Diaminopimelate Decarboxylase from m. jannaschii in co-complex with L-lysine
Overview
Cocrystal structures of Methanococcus jannaschii diaminopimelate decarboxylase (DAPDC) bound to a substrate analog, azelaic acid, and its L-lysine product have been determined at 2.6 A and 2.0 A, respectively. This PLP-dependent enzyme is responsible for the final step of L-lysine biosynthesis in bacteria and plays a role in beta-lactam antibiotic resistance in Staphylococcus aureus. Substrate specificity derives from recognition of the L-chiral center of diaminopimelate and a system of ionic "molecular rulers" that dictate substrate length. A coupled-enzyme assay system permitted measurement of kinetic parameters for recombinant DAPDCs and inhibition constants (K(i)) for azelaic acid (89 microM) and other substrate analogs. Implications for rational design of broad-spectrum antimicrobial agents targeted against DAPDCs of drug-resistant strains of bacterial pathogens, such as Staphylococcus aureus, are discussed.
About this Structure
1TWI is a Single protein structure of sequence from Methanocaldococcus jannaschii with , and as ligands. Active as Diaminopimelate decarboxylase, with EC number 4.1.1.20 Full crystallographic information is available from OCA.
Reference
Cocrystal structures of diaminopimelate decarboxylase: mechanism, evolution, and inhibition of an antibiotic resistance accessory factor., Ray SS, Bonanno JB, Rajashankar KR, Pinho MG, He G, De Lencastre H, Tomasz A, Burley SK, Structure. 2002 Nov;10(11):1499-508. PMID:12429091
Page seeded by OCA on Thu Feb 21 15:18:05 2008
Categories: Diaminopimelate decarboxylase | Methanocaldococcus jannaschii | Single protein | Bonanno, J B. | Burley, S K. | He, G. | Lencastre, H De. | NYSGXRC, New York Structural GenomiX Research Consortium. | Pinho, M G. | Rajashankar, K R. | Ray, S S. | Tomasz, A. | LYS | MG | PLP | Antibiotic resistance | Lysine biosynthesis | New york structural genomix research consortium | Nysgxrc | Protein structure initiative | Psi | Structural genomics | T135
