2pqe: Difference between revisions
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[[Image:2pqe.gif|left|200px]] | [[Image:2pqe.gif|left|200px]] | ||
'''Solution structure of proline-free mutant of staphylococcal nuclease''' | {{Structure | ||
|PDB= 2pqe |SIZE=350|CAPTION= <scene name='initialview01'>2pqe</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Micrococcal_nuclease Micrococcal nuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.31.1 3.1.31.1] | |||
|GENE= nuc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus]) | |||
}} | |||
'''Solution structure of proline-free mutant of staphylococcal nuclease''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2PQE is a [ | 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]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17887731 17887731] | ||
[[Category: Micrococcal nuclease]] | [[Category: Micrococcal nuclease]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ob fold]] | [[Category: ob 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 18:16:10 2008'' | ||
Revision as of 16:16, 20 March 2008
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| 2pqe | |||||||||||||
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| Gene: | nuc (Staphylococcus aureus) | ||||||||||||
| Activity: | Micrococcal nuclease, with EC number 3.1.31.1 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Solution structure of proline-free mutant of staphylococcal nuclease
Overview
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.
About this Structure
2PQE is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic 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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