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| | {{STRUCTURE_1tla| PDB=1tla | SCENE= }} | | {{STRUCTURE_1tla| PDB=1tla | SCENE= }} |
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| - | '''HYDROPHOBIC CORE REPACKING AND AROMATIC-AROMATIC INTERACTION IN THE THERMOSTABLE MUTANT OF T4 LYSOZYME SER 117 (RIGHT ARROW) PHE'''
| + | ===HYDROPHOBIC CORE REPACKING AND AROMATIC-AROMATIC INTERACTION IN THE THERMOSTABLE MUTANT OF T4 LYSOZYME SER 117 (RIGHT ARROW) PHE=== |
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| - | ==Overview==
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| - | The T4 lysozyme mutant Ser 117-->Phe was isolated fortuitously and found to be more thermostable than wild-type by 1.1-1.4 kcal/mol. In the wild-type structure, the side chain of Ser 117 is in a sterically restricted region near the protein surface and forms a short hydrogen bond with Asn 132. The crystal structure of the S117F mutant shows that the introduced Phe side chain rotates by about 150 degrees about the C alpha-C beta bond relative to wild type and is buried in the hydrophobic core of the protein. Burial of Phe 117 is accommodated by rearrangements of the surrounding side chains of Leu 121, Leu 133, and Phe 153 and by main-chain shifts, which result in a minimal increase in packing density. The benzyl rings of Phe 117 and Phe 153 form a near-optimal edge-face interaction in the mutant structure. This aromatic-aromatic interaction, as well as increased hydrophobic stabilization and elimination of a close contact in the wild-type protein, apparently compensate for the loss of a hydrogen bond and the possible cost of structural rearrangements in the mutant. The structure illustrates the ability of a protein to accommodate a surprisingly large structural change in a manner that actually increases thermal stability. The mutant has activity about 10% that of wild-type, supportive of the prior hypothesis (Grutter, M.G. & Matthews, B.W., 1982, J. Mol. Biol. 154, 525-535) that the peptidoglycan substrate of T4 lysozyme makes extended contacts with the C-terminal domain in the vicinity of Ser 117.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8401213}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8401213 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8401213}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Matthews, B W.]] | | [[Category: Matthews, B W.]] |
| | [[Category: Nicholson, H.]] | | [[Category: Nicholson, H.]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:05:19 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:57:29 2008'' |
Revision as of 12:57, 29 July 2008
Template:STRUCTURE 1tla
HYDROPHOBIC CORE REPACKING AND AROMATIC-AROMATIC INTERACTION IN THE THERMOSTABLE MUTANT OF T4 LYSOZYME SER 117 (RIGHT ARROW) PHE
Template:ABSTRACT PUBMED 8401213
About this Structure
1TLA is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.
Reference
Hydrophobic core repacking and aromatic-aromatic interaction in the thermostable mutant of T4 lysozyme Ser 117-->Phe., Anderson DE, Hurley JH, Nicholson H, Baase WA, Matthews BW, Protein Sci. 1993 Aug;2(8):1285-90. PMID:8401213
Page seeded by OCA on Tue Jul 29 15:57:29 2008
