View source for 1idp


==Crystal structure of scytalone dehydratase F162A mutant in the unligated state==
<StructureSection load='1idp' size='340' side='right'caption='[[1idp]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45&#8491;</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>
</table>
== Function ==
[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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/id/1idp_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1idp ConSurf].
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== 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<ref>PMID:11752795</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyricularia grisea]]
[[Category: Motoyama T]]
[[Category: Nakasako M]]
[[Category: Yamaguchi I]]