1keb: Difference between revisions
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'''Crystal Structure of Double Mutant M37L,P40S E.coli Thioredoxin''' | {{Structure | ||
|PDB= 1keb |SIZE=350|CAPTION= <scene name='initialview01'>1keb</scene>, resolution 1.8Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CU:COPPER (II) ION'>CU</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal Structure of Double Mutant M37L,P40S E.coli Thioredoxin''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1KEB is a [ | 1KEB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KEB OCA]. | ||
==Reference== | ==Reference== | ||
Structural consequences of replacement of an alpha-helical Pro residue in Escherichia coli thioredoxin., Rudresh, Jain R, Dani V, Mitra A, Srivastava S, Sarma SP, Varadarajan R, Ramakumar S, Protein Eng. 2002 Aug;15(8):627-33. PMID:[http:// | Structural consequences of replacement of an alpha-helical Pro residue in Escherichia coli thioredoxin., Rudresh, Jain R, Dani V, Mitra A, Srivastava S, Sarma SP, Varadarajan R, Ramakumar S, Protein Eng. 2002 Aug;15(8):627-33. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12364576 12364576] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: thioredoxin fold]] | [[Category: thioredoxin fold]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:16:15 2008'' | ||
Revision as of 13:16, 20 March 2008
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Crystal Structure of Double Mutant M37L,P40S E.coli Thioredoxin
OverviewOverview
While it is well known that introduction of Pro residues into the interior of protein alpha-helices is destabilizing, there have been few studies that have examined the structural and thermodynamic effects of the replacement of a Pro residue in the interior of a protein alpha-helix. We have previously reported an increase in stability in the P40S mutant of Escherichia coli thioredoxin of 1-1.5 kcal/mol in the temperature range 280-330 K. This paper describes the structure of the P40S mutant at a resolution of 1.8 A. In wild-type thioredoxin, P40 is located in the interior of helix two, a long alpha-helix that extends from residues 32 to 49 with a kink at residue 40. Structural differences between the wild-type and P40S are largely localized to the above helix. In the P40S mutant, there is an expected additional hydrogen bond formed between the amide of S40 and the carbonyl of residue K36 and also additional hydrogen bonds between the side chain of S40 and the carbonyl of K36. The helix remains kinked. In the wild-type, main chain hydrogen bonds exist between the amide of 44 and carbonyl of 40 and between the amide of 43 and carbonyl of 39. However, these are absent in P40S. Instead, these main chain atoms are hydrogen bonded to water molecules. The increased stability of P40S is likely to be due to the net increase in the number of hydrogen bonds in helix two of E.coli thioredoxin.
About this StructureAbout this Structure
1KEB is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Structural consequences of replacement of an alpha-helical Pro residue in Escherichia coli thioredoxin., Rudresh, Jain R, Dani V, Mitra A, Srivastava S, Sarma SP, Varadarajan R, Ramakumar S, Protein Eng. 2002 Aug;15(8):627-33. PMID:12364576
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