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| - | [[Image:1keb.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1keb| PDB=1keb | SCENE= }} | | {{STRUCTURE_1keb| PDB=1keb | SCENE= }} |
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| - | '''Crystal Structure of Double Mutant M37L,P40S E.coli Thioredoxin'''
| + | ===Crystal Structure of Double Mutant M37L,P40S E.coli Thioredoxin=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12364576}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12364576 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12364576}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Proline]] | | [[Category: Proline]] |
| | [[Category: Thioredoxin fold]] | | [[Category: Thioredoxin fold]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:38:21 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:12:49 2008'' |
Revision as of 07:12, 2 July 2008
Template:STRUCTURE 1keb
Crystal Structure of Double Mutant M37L,P40S E.coli Thioredoxin
Template:ABSTRACT PUBMED 12364576
About this Structure
1KEB is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
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:12364576
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