1k1d
From Proteopedia
(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...) |
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| - | [[Image:1k1d.gif|left|200px]]<br /><applet load="1k1d" size=" | + | [[Image:1k1d.gif|left|200px]]<br /><applet load="1k1d" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1k1d, resolution 3.01Å" /> | caption="1k1d, resolution 3.01Å" /> | ||
'''Crystal structure of D-hydantoinase'''<br /> | '''Crystal structure of D-hydantoinase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Industrial production of antibiotics, such as semisynthetic penicillins | + | 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== | ==About this Structure== | ||
| - | 1K1D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1K1D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K1D OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Abendroth, J.]] | [[Category: Abendroth, J.]] | ||
| - | [[Category: Cheon, Y | + | [[Category: Cheon, Y H.]] |
| - | [[Category: Han, K | + | [[Category: Han, K H.]] |
| - | [[Category: Kim, H | + | [[Category: Kim, H S.]] |
[[Category: Kim, Y.]] | [[Category: Kim, Y.]] | ||
[[Category: Niefind, K.]] | [[Category: Niefind, K.]] | ||
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[[Category: d-hydantoinase]] | [[Category: d-hydantoinase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:28:59 2008'' |
Revision as of 11:29, 21 February 2008
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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 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
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