1twi

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|PDB= 1twi |SIZE=350|CAPTION= <scene name='initialview01'>1twi</scene>, resolution 2.00&Aring;
|PDB= 1twi |SIZE=350|CAPTION= <scene name='initialview01'>1twi</scene>, resolution 2.00&Aring;
|SITE=
|SITE=
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|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>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=LYS:LYSINE'>LYS</scene> and <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:24:10 2008''
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''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

Image:1twi.gif


PDB ID 1twi

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands: , and
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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