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1g0m

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{{STRUCTURE_1g0m| PDB=1g0m | SCENE= }}
{{STRUCTURE_1g0m| PDB=1g0m | SCENE= }}
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'''CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT T152I'''
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===CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT T152I===
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==Overview==
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To investigate the structural and thermodynamic basis of the binding of solvent at internal sites within proteins a number of mutations were constructed in T4 lysozyme. Some of these were designed to introduce new solvent-binding sites. Others were intended to displace solvent from preexisting sites. In one case Val-149 was replaced with alanine, serine, cysteine, threonine, isoleucine, and glycine. Crystallographic analysis shows that, with the exception of isoleucine, each of these substitutions results in the binding of solvent at a polar site that is sterically blocked in the wild-type enzyme. Mutations designed to perturb or displace a solvent molecule present in the native enzyme included the replacement of Thr-152 with alanine, serine, cysteine, valine, and isoleucine. Although the solvent molecule was moved in some cases by up to 1.7 A, in no case was it completely removed from the folded protein. The results suggest that hydrogen bonds from the protein to bound solvent are energy neutral. The binding of solvent to internal sites within proteins also appears to be energy neutral except insofar as the bound solvent may prevent a loss of energy due to potential hydrogen bonding groups that would otherwise be unsatisfied. The introduction of a solvent-binding site appears to require not only a cavity to accommodate the water molecule but also the presence of polar groups to help satisfy its hydrogen-bonding potential. It may be easier to design a site to accommodate two or more water molecules rather than one as the solvent molecules can then hydrogen-bond to each other. For similar reasons it is often difficult to design a point mutation that will displace a single solvent molecule from the core of a protein.
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(as it appears on PubMed at http://www.pubmed.gov), where 11316887 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11316887}}
==About this Structure==
==About this Structure==
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: O-glycosyl]]
[[Category: O-glycosyl]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:58:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:13:25 2008''

Revision as of 01:13, 1 July 2008

Image:1g0m.png

Template:STRUCTURE 1g0m

CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT T152I

Template:ABSTRACT PUBMED 11316887

About this Structure

1G0M is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.

Reference

Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme., Xu J, Baase WA, Quillin ML, Baldwin EP, Matthews BW, Protein Sci. 2001 May;10(5):1067-78. PMID:11316887

Page seeded by OCA on Tue Jul 1 04:13:25 2008

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