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1b4q

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{{STRUCTURE_1b4q| PDB=1b4q | SCENE= }}
{{STRUCTURE_1b4q| PDB=1b4q | SCENE= }}
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'''SOLUTION STRUCTURE OF HUMAN THIOLTRANSFERASE COMPLEX WITH GLUTATHIONE'''
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===SOLUTION STRUCTURE OF HUMAN THIOLTRANSFERASE COMPLEX WITH GLUTATHIONE===
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==Overview==
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Human thioltransferase (TTase) is a 12 kDa thiol-disulfide oxidoreductase that appears to play a critical role in maintaining the redox environment of the cell. TTase acts as a potent and specific reducing agent for protein-S-S-glutathione mixed disulfides (protein-SSG) likely formed during oxidative stress or as redox intermediates in signal transduction pathways. Accordingly, the catalytic cycle of thioltransferase itself involves a covalent glutathionyl enzyme disulfide intermediate (TTase-C22-SSG). To understand the molecular basis of TTase specificity for the glutathione moiety, we engineered a quadruple Cys to Ser mutant of human TTase (C7S, C25S, C78S, and C82S) which retains only the active site cysteine residue (C22), and we solved its high-resolution NMR solution structure in the mixed disulfide intermediate with glutathione (QM-TTase-SSG). This mutant which cannot form a C22-S-S-C25 intramolecular disulfide displays the same catalytic efficiency (Vmax/KM) and specificity for glutathionyl mixed disulfide substrates as wild-type TTase, indicating that the Cys-25-SH moiety is not required for catalysis or glutathionyl specificity. The structure of human thioltransferase is characterized by a thioredoxin-like fold which comprises a four-stranded central beta-sheet flanked on each side by alpha-helices. The disulfide-adducted glutathione in the TTase-SSG complex has an extended conformation and is localized in a cleft near the protein surface encompassing the residues from helices-alpha2,alpha3, the active site loop, and the loop connecting helix-alpha3 and strand-beta3. Numerous van der Waals and electrostatic interactions between the protein and the glutathione moiety are identified as contributing to stabilization of the complex and confering the substrate specificity. Comparison of the human thioltransferase with other thiol-disulfide oxidoreductases reveals structural and functional differences.
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{{ABSTRACT_PUBMED_9860827}}
==About this Structure==
==About this Structure==
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1B4Q is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B4Q OCA].
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1B4Q is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B4Q OCA].
==Reference==
==Reference==
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[[Category: Human thioltransferase]]
[[Category: Human thioltransferase]]
[[Category: Nmr]]
[[Category: Nmr]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:04:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:15:29 2008''

Revision as of 15:15, 30 June 2008

Image:1b4q.png

Template:STRUCTURE 1b4q

SOLUTION STRUCTURE OF HUMAN THIOLTRANSFERASE COMPLEX WITH GLUTATHIONE

Template:ABSTRACT PUBMED 9860827

About this Structure

1B4Q is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S, C78S, C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity., Yang Y, Jao S, Nanduri S, Starke DW, Mieyal JJ, Qin J, Biochemistry. 1998 Dec 8;37(49):17145-56. PMID:9860827

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