1twi: Difference between revisions
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|PDB= 1twi |SIZE=350|CAPTION= <scene name='initialview01'>1twi</scene>, resolution 2.00Å | |PDB= 1twi |SIZE=350|CAPTION= <scene name='initialview01'>1twi</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=LYS:LYSINE'>LYS</scene> and <scene name='pdbligand=PLP:PYRIDOXAL-5 | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=LYS:LYSINE'>LYS</scene> and <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene> | ||
|ACTIVITY= [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] | |ACTIVITY= [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] | ||
|GENE= LYSA, MJ1097 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 Methanocaldococcus jannaschii]) | |GENE= LYSA, MJ1097 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 Methanocaldococcus jannaschii]) | ||
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[[Category: t135]] | [[Category: t135]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 13:47:44 2008'' | ||
Revision as of 11:47, 23 March 2008
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| 1twi, resolution 2.00Å | |||||||||||||
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| Ligands: | MG, LYS and PLP | ||||||||||||
| Gene: | LYSA, MJ1097 (Methanocaldococcus jannaschii) | ||||||||||||
| Activity: | Diaminopimelate decarboxylase, with EC number 4.1.1.20 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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
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Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- 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 genomic
- T135
