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| | {{STRUCTURE_1huv| PDB=1huv | SCENE= }} | | {{STRUCTURE_1huv| PDB=1huv | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF A SOLUBLE MUTANT OF THE MEMBRANE-ASSOCIATED (S)-MANDELATE DEHYDROGENASE FROM PSEUDOMONAS PUTIDA AT 2.15A RESOLUTION'''
| + | ===CRYSTAL STRUCTURE OF A SOLUBLE MUTANT OF THE MEMBRANE-ASSOCIATED (S)-MANDELATE DEHYDROGENASE FROM PSEUDOMONAS PUTIDA AT 2.15A RESOLUTION=== |
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| - | ==Overview==
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| - | The structure of an active mutant of (S)-mandelate dehydrogenase (MDH-GOX2) from Pseudomonas putida has been determined at 2.15 A resolution. The membrane-associated flavoenzyme (S)-mandelate dehydrogenase (MDH) catalyzes the oxidation of (S)-mandelate to give a flavin hydroquinone intermediate which is subsequently reoxidized by an organic oxidant residing in the membrane. The enzyme was rendered soluble by replacing its 39-residue membrane-binding peptide segment with a corresponding 20-residue segment from its soluble homologue, glycolate oxidase (GOX). Because of their amphipathic nature and peculiar solubilization properties, membrane proteins are notoriously difficult to crystallize, yet represent a large fraction of the proteins encoded by genomes currently being deciphered. Here we present the first report of such a structure in which an internal membrane-binding segment has been replaced, leading to successful crystallization of the fully active enzyme in the absence of detergents. This approach may have general application to other membrane-bound proteins. The overall fold of the molecule is that of a TIM barrel, and it forms a tight tetramer within the crystal lattice that has circular 4-fold symmetry. The structure of MDH-GOX2 reveals how this molecule can interact with a membrane, although it is limited by the absence of a membrane-binding segment. MDH-GOX2 and GOX adopt similar conformations, yet they retain features characteristic of membrane and globular proteins, respectively. MDH-GOX2 has a distinctly electropositive surface capable of interacting with the membrane, while the opposite surface is largely electronegative. GOX shows no such pattern. MDH appears to form a new class of monotopic integral membrane protein that interacts with the membrane through coplanar electrostatic binding surfaces and hydrophobic interactions, thus combining features of both the prostaglandin synthase/squaline-hopine cyclase and the C-2 coagulation factor domain classes of membrane proteins.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11502180}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11502180 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11502180}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Sukumar, N.]] | | [[Category: Sukumar, N.]] |
| | [[Category: Tim barrel]] | | [[Category: Tim barrel]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:15:18 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:46:01 2008'' |
Revision as of 05:46, 1 July 2008
Template:STRUCTURE 1huv
CRYSTAL STRUCTURE OF A SOLUBLE MUTANT OF THE MEMBRANE-ASSOCIATED (S)-MANDELATE DEHYDROGENASE FROM PSEUDOMONAS PUTIDA AT 2.15A RESOLUTION
Template:ABSTRACT PUBMED 11502180
About this Structure
1HUV is a Single protein structure of sequence from Pseudomonas putida. Full crystallographic information is available from OCA.
Reference
Structure of an active soluble mutant of the membrane-associated (S)-mandelate dehydrogenase., Sukumar N, Xu Y, Gatti DL, Mitra B, Mathews FS, Biochemistry. 2001 Aug 21;40(33):9870-8. PMID:11502180
Page seeded by OCA on Tue Jul 1 08:46:01 2008
