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2pqe

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[[Image:2pqe.gif|left|200px]]
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{{STRUCTURE_2pqe| PDB=2pqe | SCENE= }}
{{STRUCTURE_2pqe| PDB=2pqe | SCENE= }}
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'''Solution structure of proline-free mutant of staphylococcal nuclease'''
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===Solution structure of proline-free mutant of staphylococcal nuclease===
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==Overview==
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The role of cis-trans isomerizations of peptidyl-proline bonds in the enzyme activity of staphylococcal nuclease (SNase) was examined by mutation of proline residues. The proline-free SNase ([Pro-]SNase), namely, P11A/P31A/P42A/P47T/P56A/P117G-mutant SNase, was adopted for elucidating the correlation between the nuclease activity and the backbone conformational and dynamic states of SNase. The 3D solution structure of [Pro-]SNase has been determined by heteronuclear NMR experiments. Comparing the structure of [Pro-]SNase with the structure of SNase revealed the conformational differences between the two proteins. In the structure of [Pro-]SNase, conformational rearrangements were observed for the loop of residues Ala112-His121 containing a trans Lys116-Gly117 peptide bond and for the C-terminal alpha-helical loop of residues Leu137-Glu142. Mutation of proline at position 117 also caused the conformational rearrangement of the p-loop (Asp77-Leu89), which is remote from the Ala112-His121 loop. The Ala112-His121 loop and p-loop are placed closer to each other in [Pro-]SNase than in SNase. The backbone dynamic features of the omega-loop (Pro42-Pro56) of SNase are different from those of [Pro-]SNase. The backbone of the omega-loop exhibits restricted flexibility with slow conformational exchange motions in SNase, but is highly flexible in [Pro-]SNase. The analysis indicates that the restrained backbone conformation of the Ala112-His121 loop and restricted flexibility of the omega-loop are two dominant factors determining the enzyme activity of SNase. Of the two factors, the former is correlated with the strained cis Lys116-Pro117 peptide bond and the latter is correlated with the cis-trans isomerizations of the His46-Pro47 peptide bond.
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(as it appears on PubMed at http://www.pubmed.gov), where 17887731 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17887731}}
==About this Structure==
==About this Structure==
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2PQE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PQE OCA].
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2PQE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PQE OCA].
==Reference==
==Reference==
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Ob fold]]
[[Category: Ob fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:37:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:06:32 2008''

Revision as of 09:06, 29 July 2008

Image:2pqe.png

Template:STRUCTURE 2pqe

Solution structure of proline-free mutant of staphylococcal nuclease

Template:ABSTRACT PUBMED 17887731

About this Structure

2PQE is a Single protein structure of sequence from Staphylococcus aureus. Full experimental information is available from OCA.

Reference

Restricted backbone conformational and motional flexibilities of loops containing peptidyl-proline bonds dominate the enzyme activity of staphylococcal nuclease., Shan L, Tong Y, Xie T, Wang M, Wang J, Biochemistry. 2007 Oct 16;46(41):11504-13. Epub 2007 Sep 22. PMID:17887731

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