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| | ==Crystal structure of scytalone dehydratase F162A mutant in the unligated state== | | ==Crystal structure of scytalone dehydratase F162A mutant in the unligated state== |
| - | <StructureSection load='1idp' size='340' side='right' caption='[[1idp]], [[Resolution|resolution]] 1.45Å' scene=''> | + | <StructureSection load='1idp' size='340' side='right'caption='[[1idp]], [[Resolution|resolution]] 1.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1idp]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_138707_[[pyricularia_grisea]] Cbs 138707 [[pyricularia grisea]]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IDP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IDP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1idp]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyricularia_grisea Pyricularia grisea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IDP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IDP FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3std|3std]], [[4std|4std]], [[5std|5std]], [[6std|6std]], [[7std|7std]]</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]] 1.45Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Scytalone_dehydratase Scytalone dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.94 4.2.1.94] </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=1idp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1idp OCA], [https://pdbe.org/1idp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1idp RCSB], [https://www.ebi.ac.uk/pdbsum/1idp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1idp ProSAT]</span></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=1idp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1idp OCA], [http://pdbe.org/1idp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1idp RCSB], [http://www.ebi.ac.uk/pdbsum/1idp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1idp ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SCYD_MAGO7 SCYD_MAGO7]] Catalyzes two steps in melanin biosynthesis. From scytalone they are two dehydration steps and one reduction step to yield melanin. | + | [https://www.uniprot.org/uniprot/SCYD_MAGO7 SCYD_MAGO7] Catalyzes two steps in melanin biosynthesis. From scytalone they are two dehydration steps and one reduction step to yield melanin. |
| | == 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: Scytalone dehydratase]] | + | [[Category: Large Structures]] |
| - | [[Category: Motoyama, T]] | + | [[Category: Pyricularia grisea]] |
| - | [[Category: Nakasako, M]] | + | [[Category: Motoyama T]] |
| - | [[Category: Yamaguchi, I]] | + | [[Category: Nakasako M]] |
| - | [[Category: Lyase]] | + | [[Category: Yamaguchi I]] |
| - | [[Category: Melanine biosynthesis]]
| + | |
| Structural highlights
Function
SCYD_MAGO7 Catalyzes two steps in melanin biosynthesis. From scytalone they are two dehydration steps and one reduction step to yield melanin.
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
Scytalone dehydratase variant F162A, in which Phe162 in the C-terminal region was replaced with alanine, was crystallized with polyethylene glycol 4000. Because the crystal was radiation-sensitive, the diffraction data were collected at cryogenic temperatures. The crystal belonged to monoclinic space group P2(1), with unit-cell parameters a = 72.64, b = 61.30, c = 72.62 A, beta = 120.02 degrees at 37 K. The calculated V(M) value was acceptable when a trimer of the mutant enzyme occupied a crystallographic asymmetric unit. The resolution limit was extended to 1.45 A at BL41XU of SPring-8 at 37 K.
Crystallization of scytalone dehydratase F162A mutant in the unligated state and a preliminary X-ray diffraction study at 37 K.,Motoyama T, Nakasako M, Yamaguchi I Acta Crystallogr D Biol Crystallogr. 2002 Jan;58(Pt 1):148-50. Epub 2001, Dec 21. PMID:11752795[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Motoyama T, Nakasako M, Yamaguchi I. Crystallization of scytalone dehydratase F162A mutant in the unligated state and a preliminary X-ray diffraction study at 37 K. Acta Crystallogr D Biol Crystallogr. 2002 Jan;58(Pt 1):148-50. Epub 2001, Dec 21. PMID:11752795
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