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1bri

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[[Image:1bri.gif|left|200px]]
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{{STRUCTURE_1bri| PDB=1bri | SCENE= }}
{{STRUCTURE_1bri| PDB=1bri | SCENE= }}
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'''BARNASE MUTANT WITH ILE 76 REPLACED BY ALA'''
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===BARNASE MUTANT WITH ILE 76 REPLACED BY ALA===
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==Overview==
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We have solved the 2.0-A resolution crystal structures of four cavity-creating Ile/Leu--&gt;Ala mutations in the hydrophobic core of barnase and compare and contrast the structural responses to mutation with those found for Leu--&gt;Ala mutations in T4 lysozyme. First, there are rearrangements of structure of barnase that cause the cavities to collapse partly, and there is an approximately linear relationship between the changes in stability and the volume of the cavity similar to that found for the mutants of T4 lysozyme. Second, although it is currently accepted that hydrophobic cavities formed on the mutation of large hydrophobic side chains to smaller ones are not occupied by water molecules, we found a buried water molecule in the crystal structure of the barnase mutant Ile76--&gt;Ala. A single hydrogen bond is formed between the water molecule and a polar atom, the carbonyl oxygen of Phe7, in the hydrophobic cavity that is formed on mutation. A survey of hydrophobic cavities produced by similar mutations in different proteins reveals that they all contain a proportion of polar atoms in their linings. The availability of such polar sites has implications for understanding folding pathways because a solvated core is presumed present in the transition state for folding and unfolding. Notably, the hydrogen bond between the cavity-water and the carbonyl group of Phe7 is also a marked early feature of very recent molecular dynamics simulations of barnase denaturation [Caflisch, A., &amp; Karplus, M. (1995) J. Mol. Biol. 252, 672-708]. It is possible that cavities engineered into the hydrophobic cores of other proteins may contain water molecules, even though they cannot be detected by crystallographic analysis.
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(as it appears on PubMed at http://www.pubmed.gov), where 8605178 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8605178}}
==About this Structure==
==About this Structure==
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[[Category: Fersht, A.]]
[[Category: Fersht, A.]]
[[Category: Alpha/beta protein alpha/beta protein]]
[[Category: Alpha/beta protein alpha/beta protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:52:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:36:34 2008''

Revision as of 16:36, 30 June 2008

Image:1bri.png

Template:STRUCTURE 1bri

BARNASE MUTANT WITH ILE 76 REPLACED BY ALA

Template:ABSTRACT PUBMED 8605178

About this Structure

1BRI is a Single protein structure of sequence from Bacillus amyloliquefaciens. Full crystallographic information is available from OCA.

Reference

Structural and energetic responses to cavity-creating mutations in hydrophobic cores: observation of a buried water molecule and the hydrophilic nature of such hydrophobic cavities., Buckle AM, Cramer P, Fersht AR, Biochemistry. 1996 Apr 9;35(14):4298-305. PMID:8605178

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