208l: Difference between revisions

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[[Image:208l.jpg|left|200px]]
[[Image:208l.jpg|left|200px]]


{{Structure
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=208l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=208l OCA], [http://www.ebi.ac.uk/pdbsum/208l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=208l RCSB]</span>
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'''MUTANT HUMAN LYSOZYME C77A'''
'''MUTANT HUMAN LYSOZYME C77A'''
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[[Category: Matsushima, M.]]
[[Category: Matsushima, M.]]
[[Category: Song, H.]]
[[Category: Song, H.]]
[[Category: complex (hydrolase (o-glycosyl)/cys)]]
[[Category: Hydrolase]]
[[Category: hydrolase]]
[[Category: Mutant human lysozyme]]
[[Category: mutant human lysozyme]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 18:18:11 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:44:05 2008''

Revision as of 18:18, 3 May 2008

File:208l.jpg

Template:STRUCTURE 208l

MUTANT HUMAN LYSOZYME C77A


OverviewOverview

We previously reported that protein disulfide isomerase (PDI) can dissociate the glutathione molecule in vitro from the mutant human lysozyme (hLZM) C77A-a, which is modified with glutathione at Cys95; however, it seems structurally difficult for PDI to attack either the disulfide bond or the side chain of the cysteine residue of a mixed disulfide. To investigate the function of PDI, we introduced several glutathione and cysteine derivatives at Cys95, instead of the glutathione of C77A-a. Using thiol compounds modified by 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB), we could easily modify the free thiol group of C77A-b (C77A with no glutathionylation), without denaturation. For all of the modifications we tested, a negative correlation was found between the initial rate and the acceleration ratio of the reductive cleavage of mixed disulfides with PDI. A mutant PDI (hPDIM), which has no thiol-disulfide exchange activity, suppressed the reductive cleavage of the mixed disulfide of C77A-a with hPDI, suggesting that hPDI non-covalently interacted with the substrates. Taking account of the results of the structural analysis, we conclude that one of the functions of PDI in vivo lies in relaxing the structure around the disulfide bond, as well as in exchanging the thiol-disulfide bonds.

About this StructureAbout this Structure

208L is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

A role of PDI in the reductive cleavage of mixed disulfides., Nakamura S, Matsushima M, Song H, Kikuchi M, J Biochem. 1996 Sep;120(3):525-30. PMID:8902616 Page seeded by OCA on Sat May 3 18:18:11 2008

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