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| | ==Crystal structure of fusion protein of MsrA and MsrB== | | ==Crystal structure of fusion protein of MsrA and MsrB== |
| - | <StructureSection load='3e0m' size='340' side='right' caption='[[3e0m]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='3e0m' size='340' side='right'caption='[[3e0m]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3e0m]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/"diplococcus_pneumoniae"_(klein_1884)_weichselbaum_1886 "diplococcus pneumoniae" (klein 1884) weichselbaum 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E0M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3E0M FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3e0m]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/"diplococcus_pneumoniae"_(klein_1884)_weichselbaum_1886 "diplococcus pneumoniae" (klein 1884) weichselbaum 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E0M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E0M FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">msrAB1, exp3, msrA, SP_1359 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1313 "Diplococcus pneumoniae" (Klein 1884) Weichselbaum 1886])</td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">msrAB1, exp3, msrA, SP_1359 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1313 "Diplococcus pneumoniae" (Klein 1884) Weichselbaum 1886])</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3e0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e0m OCA], [http://pdbe.org/3e0m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3e0m RCSB], [http://www.ebi.ac.uk/pdbsum/3e0m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3e0m ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3e0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e0m OCA], [https://pdbe.org/3e0m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e0m RCSB], [https://www.ebi.ac.uk/pdbsum/3e0m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e0m ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MSAB1_STRPN MSAB1_STRPN]] Has an important function as a repair enzyme for proteins that have been inactivated by oxidation (By similarity). Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity). | + | [[https://www.uniprot.org/uniprot/MSAB1_STRPN MSAB1_STRPN]] Has an important function as a repair enzyme for proteins that have been inactivated by oxidation (By similarity). Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Hwang, K Y]] | | [[Category: Hwang, K Y]] |
| | [[Category: Kim, Y K]] | | [[Category: Kim, Y K]] |
| Structural highlights
Function
[MSAB1_STRPN] Has an important function as a repair enzyme for proteins that have been inactivated by oxidation (By similarity). Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Methionine sulphoxide reductases (Msr) catalyse the reduction of oxidized methionine to methionine. These enzymes are divided into two classes, MsrA and MsrB, according to substrate specificity. Although most MsrA and MsrB exist as separate enzymes, in some bacteria these two enzymes are fused to form a single polypeptide (MsrAB). Here, we report the first crystal structure of MsrAB from Streptococcus pneumoniae (SpMsrAB) at 2.4 A resolution. SpMsrAB consists of an N-terminal MsrA domain, a C-terminal MsrB domain and a linker. The linker is composed of 13 residues and contains one 3(10)-helix and several hydrogen bonds interacting with both MsrA and MsrB domains. Interestingly, our structure includes the MsrB domain complexed with an SHMAEI hexa-peptide that is the N-terminal region of neighbouring MsrA domain. A kinetic analysis showed that the apparent K(m) of SpMsrAB for the R-form-substrate was 20-fold lower than that for the S-form substrate, indicating that the MsrB domain had a much higher affinity for the substrate than the MsrA domain. Our study reveals the first structure of the MsrAB by providing insights into the formation of a disulphide bridge in the MsrB, the structure of the linker region, and the distinct structural nature of active site of each MsrA and MsrB domain.
Structural and kinetic analysis of an MsrA-MsrB fusion protein from Streptococcus pneumoniae.,Kim YK, Shin YJ, Lee WH, Kim HY, Hwang KY Mol Microbiol. 2009 May;72(3):699-709. Epub 2009 Apr 7. PMID:19400786[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kim YK, Shin YJ, Lee WH, Kim HY, Hwang KY. Structural and kinetic analysis of an MsrA-MsrB fusion protein from Streptococcus pneumoniae. Mol Microbiol. 2009 May;72(3):699-709. Epub 2009 Apr 7. PMID:19400786 doi:10.1111/j.1365-2958.2009.06680.x
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