1uh7

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{{STRUCTURE_1uh7| PDB=1uh7 | SCENE= }}
{{STRUCTURE_1uh7| PDB=1uh7 | SCENE= }}
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'''Crystal structure of rhizopuspepsin at pH 4.6'''
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===Crystal structure of rhizopuspepsin at pH 4.6===
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==Overview==
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The crystal structure of rhizopuspepsin has been determined at three different pH values (4.6, 7.0 and 8.0) and compared with the previously reported structure at pH 6.0. A pH-sensitive region in the protein has been identified where certain structural changes take place at pH 8.0. An increase in the mobility of loops, weakening of hydrogen bonding and ionic interactions and a change in the water structure have been observed in this region. The loop between the first and the second beta-strands of the N-terminus shows increased mobility at high pH. This loop is known to be highly flexible in aspartic proteinases, aiding in relocating the N-terminal beta-strand segment in pH-related structural transformations. The observed changes in rhizopuspepsin indicate the triggering of a possible denatured state by high pH. The conformation of the active aspartates and the geometry of the catalytic site exhibit remarkable rigidity in this pH range.
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(as it appears on PubMed at http://www.pubmed.gov), where 14501114 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14501114}}
==About this Structure==
==About this Structure==
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[[Category: Aspartic proteinase]]
[[Category: Aspartic proteinase]]
[[Category: Pepsin]]
[[Category: Pepsin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:28:11 2008''

Revision as of 10:28, 27 July 2008

Template:STRUCTURE 1uh7

Crystal structure of rhizopuspepsin at pH 4.6

Template:ABSTRACT PUBMED 14501114

About this Structure

1UH7 is a Single protein structure of sequence from Rhizopus microsporus var. chinensis. Full crystallographic information is available from OCA.

Reference

Effect of pH on the structure of rhizopuspepsin., Prasad BV, Suguna K, Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1755-61. Epub 2003, Sep 19. PMID:14501114

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