1k1d
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1k1d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k1d, resolution 3.01Å" /> '''Crystal structure of...)
Next diff →
Revision as of 16:39, 20 November 2007
|
Crystal structure of D-hydantoinase
Overview
Industrial production of antibiotics, such as semisynthetic penicillins, and cephalosporins, requires optically pure D-p-hydroxylphenylglycine and, its derivatives as important side-chain precursors. To produce optically, pure D-amino acids, microbial D-hydantoinase (E.C. 3.5.2.2) is used for, stereospecific hydrolysis of chemically synthesized cyclic hydantoins. We, report the apo-crystal structure of D-hydantoinase from B., stearothermophilus SD1 at 3.0 A resolution. The structure has a classic, TIM barrel fold. Despite an undetectable similarity in sequence, D-hydantoinase shares a striking structural similarity with the recently, solved structure of dihydroorotase. A structural comparison of, hydantoinase with dihydroorotase revealed that the catalytic chemistry is, conserved, while the substrate recognition is not. This structure provides, insight into the stereochemistry of enantioselectivity in hydrolysis and, illustrates how the enzyme recognizes stereospecific exocyclic, substituents and hydrolyzes hydantoins. It should also provide a rationale, for further directed evolution of this enzyme for hydrolysis of new, hydantoins with novel exocyclic substituents.
About this Structure
1K1D is a Single protein structure of sequence from Geobacillus stearothermophilus with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of D-hydantoinase from Bacillus stearothermophilus: insight into the stereochemistry of enantioselectivity., Cheon YH, Kim HS, Han KH, Abendroth J, Niefind K, Schomburg D, Wang J, Kim Y, Biochemistry. 2002 Jul 30;41(30):9410-7. PMID:12135362
Page seeded by OCA on Tue Nov 20 18:46:12 2007
