1fy9: Difference between revisions
New page: left|200px<br /><applet load="1fy9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fy9, resolution 2.20Å" /> '''CRYSTAL STRUCTURE OF... |
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[[Image:1fy9.jpg|left|200px]]<br /><applet load="1fy9" size=" | [[Image:1fy9.jpg|left|200px]]<br /><applet load="1fy9" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1fy9, resolution 2.20Å" /> | caption="1fy9, resolution 2.20Å" /> | ||
'''CRYSTAL STRUCTURE OF THE HEXA-SUBSTITUTED MUTANT OF THE MOLECULAR CHAPERONIN GROEL APICAL DOMAIN'''<br /> | '''CRYSTAL STRUCTURE OF THE HEXA-SUBSTITUTED MUTANT OF THE MOLECULAR CHAPERONIN GROEL APICAL DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
We report the crystal structures of two hexa-substituted mutants of a | 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. | ||
==About this Structure== | ==About this Structure== | ||
1FY9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1FY9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FY9 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Buckle, A | [[Category: Buckle, A M.]] | ||
[[Category: Fersht, A | [[Category: Fersht, A R.]] | ||
[[Category: Wang, Q.]] | [[Category: Wang, Q.]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
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[[Category: stabilizing mutant]] | [[Category: stabilizing mutant]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:43:56 2008'' | ||
Revision as of 13:44, 21 February 2008
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CRYSTAL STRUCTURE OF THE HEXA-SUBSTITUTED MUTANT OF THE MOLECULAR CHAPERONIN GROEL APICAL DOMAIN
OverviewOverview
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.
About this StructureAbout this Structure
1FY9 is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
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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