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| | <StructureSection load='5fzp' size='340' side='right'caption='[[5fzp]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='5fzp' size='340' side='right'caption='[[5fzp]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5fzp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_mobaraensis Streptomyces mobaraensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FZP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FZP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5fzp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_mobaraensis Streptomyces mobaraensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FZP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FZP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5fzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fzp OCA], [http://pdbe.org/5fzp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fzp RCSB], [http://www.ebi.ac.uk/pdbsum/5fzp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fzp ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=5fzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fzp OCA], [https://pdbe.org/5fzp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fzp RCSB], [https://www.ebi.ac.uk/pdbsum/5fzp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fzp ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DAIP_STRMB DAIP_STRMB]] Induces autolysis of dispase and thermolysin.<ref>PMID:19420706</ref> | + | [https://www.uniprot.org/uniprot/DAIP_STRMB DAIP_STRMB] Induces autolysis of dispase and thermolysin.<ref>PMID:19420706</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Streptomyces mobaraensis]] | | [[Category: Streptomyces mobaraensis]] |
| - | [[Category: Beck, J]] | + | [[Category: Beck J]] |
| - | [[Category: Fiebig, D]] | + | [[Category: Fiebig D]] |
| - | [[Category: Fuchsbauer, H L]] | + | [[Category: Fuchsbauer HL]] |
| - | [[Category: Schmelz, S]] | + | [[Category: Schmelz S]] |
| - | [[Category: Scrima, A]] | + | [[Category: Scrima A]] |
| - | [[Category: 7-bladed beta-propeller]]
| + | |
| - | [[Category: Daip]]
| + | |
| - | [[Category: Dispase-autolysis inducing protein]]
| + | |
| - | [[Category: Glutamine cross- linking site]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
Function
DAIP_STRMB Induces autolysis of dispase and thermolysin.[1]
Publication Abstract from PubMed
Transglutaminase from Streptomyces mobaraensis (MTG) is an important enzyme for cross-linking and modifying proteins. An intrinsic substrate of MTG is the dispase autolysis inducing protein (DAIP). The amino acid sequence of DAIP contains five potential glutamines and ten lysines for MTG mediated cross-linking. Aim of the study was to determine the structure and glutamine cross-linking sites of the first physiological MTG substrate. A production procedure was established in E. coli BL21 (DE3) to obtain high yields of recombinant DAIP. DAIP variants were prepared by replacing four out of five glutamines for asparagines in various combinations via site-directed mutagenesis. Incorporation of biotin cadaverine revealed preference of MTG for the DAIP glutamines in the order of Q39>>Q298>Q345~Q65>>Q144. In the structure of DAIP the preferred glutamines do cluster at the top of the seven-bladed beta-propeller. This suggests a targeted cross-linking of DAIP by MTG that may occur after self-assembly in the bacterial cell wall. Based on our biochemical and the structural data of the first physiological MTG substrate, we further provide novel insight into determinants of MTG-mediated modification, specificity and efficiency.
Structure of the Dispase Autolysis Inducing Protein from Streptomyces mobaraensis and Glutamine Cross-linking Sites for Transglutaminase.,Fiebig D, Schmelz S, Zindel S, Ehret V, Beck J, Ebenig A, Ehret M, Frols S, Pfeifer F, Kolmar H, Fuchsbauer HL, Scrima A J Biol Chem. 2016 Aug 4. pii: jbc.M116.731109. PMID:27493205[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sarafeddinov A, Schmidt S, Adolf F, Mainusch M, Bender A, Fuchsbauer HL. A novel transglutaminase substrate from Streptomyces mobaraensis triggers autolysis of neutral metalloproteases. Biosci Biotechnol Biochem. 2009 May;73(5):993-9. Epub 2009 May 7. PMID:19420706 doi:http://dx.doi.org/10.1271/bbb.80769
- ↑ Fiebig D, Schmelz S, Zindel S, Ehret V, Beck J, Ebenig A, Ehret M, Frols S, Pfeifer F, Kolmar H, Fuchsbauer HL, Scrima A. Structure of the Dispase Autolysis Inducing Protein from Streptomyces mobaraensis and Glutamine Cross-linking Sites for Transglutaminase. J Biol Chem. 2016 Aug 4. pii: jbc.M116.731109. PMID:27493205 doi:http://dx.doi.org/10.1074/jbc.M116.731109
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