1s5t

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[[Image:1s5t.gif|left|200px]]
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{{STRUCTURE_1s5t| PDB=1s5t | SCENE= }}
{{STRUCTURE_1s5t| PDB=1s5t | SCENE= }}
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'''Crystal Structure Analysis of a mutant of DIHYDRODIPICOLINATE SYNTHASE--residue thr44 to val44'''
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===Crystal Structure Analysis of a mutant of DIHYDRODIPICOLINATE SYNTHASE--residue thr44 to val44===
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==Overview==
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Dihydrodipicolinate synthase (DHDPS, EC 4.2.1.52) catalyses the branchpoint reaction of lysine biosynthesis in plants and microbes: the condensation of (S)-aspartate-beta-semialdehyde and pyruvate. The crystal structure of wild-type DHDPS has been published to 2.5A, revealing a tetrameric molecule comprised of four identical (beta/alpha)(8)-barrels, each containing one active site. Previous workers have hypothesised that the catalytic mechanism of the enzyme involves a catalytic triad of amino acid residues, Tyr133, Thr44 and Tyr107, which provide a proton shuttle to transport protons from the active site to solvent. We have tested this hypothesis using site-directed mutagenesis to produce three mutant enzymes: DHDPS-Y133F, DHDPS-T44V and DHDPS-Y107F. Each of these mutants has substantially reduced activity, consistent with the catalytic triad hypothesis. We have determined each mutant crystal structure to at least 2.35A resolution and compared the structures to the wild-type enzyme. All mutant enzymes crystallised in the same space group as the wild-type form and only minor differences in structure are observed. These results suggest that the catalytic triad is indeed in operation in wild-type DHDPS.
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The line below this paragraph, {{ABSTRACT_PUBMED_15066435}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15066435 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15066435}}
==About this Structure==
==About this Structure==
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[[Category: Dihydrodipicolinate]]
[[Category: Dihydrodipicolinate]]
[[Category: Synthase]]
[[Category: Synthase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:20:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:36:35 2008''

Revision as of 11:36, 28 July 2008

Image:1s5t.png

Template:STRUCTURE 1s5t

Crystal Structure Analysis of a mutant of DIHYDRODIPICOLINATE SYNTHASE--residue thr44 to val44

Template:ABSTRACT PUBMED 15066435

About this Structure

1S5T is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The crystal structure of three site-directed mutants of Escherichia coli dihydrodipicolinate synthase: further evidence for a catalytic triad., Dobson RC, Valegard K, Gerrard JA, J Mol Biol. 2004 Apr 23;338(2):329-39. PMID:15066435

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