1fy9

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{{STRUCTURE_1fy9| PDB=1fy9 | SCENE= }}
{{STRUCTURE_1fy9| PDB=1fy9 | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE HEXA-SUBSTITUTED MUTANT OF THE MOLECULAR CHAPERONIN GROEL APICAL DOMAIN'''
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===CRYSTAL STRUCTURE OF THE HEXA-SUBSTITUTED MUTANT OF THE MOLECULAR CHAPERONIN GROEL APICAL DOMAIN===
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==Overview==
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We report the crystal structures of two hexa-substituted mutants of a GroEL minichaperone that are more stable than wild-type by 7.0 and 6.1 kcal mol(-1). Their structures imply that the increased stability results from multiple factors including improved hydrophobic packing, optimised hydrogen bonding and favourable structural rearrangements. It is commonly believed that protein core residues are immutable and generally optimized for energy, while on the contrary, surface residues are variable and hence unimportant for stability. But, it is now becoming clear that mutations of both core and surface residues can increase protein stability, and that protein cores are more flexible and thus more tolerant to mutation than expected. Sequence comparison of homologous proteins has provided a way to pinpoint the residues that contribute constructively to stability and to guide the engineering of protein stability. Stabilizing mutations identified by this approach are most frequently located at protein surfaces but with a few found in protein cores. In the latter case, local flexibility in the hydrophobic core is the key factor that allows the energetically favourable burial of larger hydrophobic side-chains without undue energetic penalties from steric clashes.
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(as it appears on PubMed at http://www.pubmed.gov), where 10801358 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10801358}}
==About this Structure==
==About this Structure==
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[[Category: Chaperone]]
[[Category: Chaperone]]
[[Category: Stabilizing mutant]]
[[Category: Stabilizing mutant]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:54:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:07:19 2008''

Revision as of 01:07, 1 July 2008

Image:1fy9.png

Template:STRUCTURE 1fy9

CRYSTAL STRUCTURE OF THE HEXA-SUBSTITUTED MUTANT OF THE MOLECULAR CHAPERONIN GROEL APICAL DOMAIN

Template:ABSTRACT PUBMED 10801358

About this Structure

1FY9 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Stabilization of GroEL minichaperones by core and surface mutations., Wang Q, Buckle AM, Fersht AR, J Mol Biol. 2000 May 19;298(5):917-26. PMID:10801358

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