3oml

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[[Image:3oml.png|left|200px]]
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==Structure of full-length peroxisomal multifunctional enzyme type 2 from Drosophila melanogaster==
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<StructureSection load='3oml' size='340' side='right' caption='[[3oml]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3oml]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OML OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OML FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CG3415, Dmel_CG3415 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster])</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3oml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oml OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3oml RCSB], [http://www.ebi.ac.uk/pdbsum/3oml PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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All the peroxisomal beta-oxidation pathways characterized thus far house at least one multifunctional enzyme (MFE) catalyzing two out of four reactions of the spiral. MFE type 2 proteins from various species display great variation in domain composition and predicted substrate preference. The gene CG3415 encodes for D. melanogaster MFE-2 (DmMFE-2), complements the S. cerevisiae MFE-2 deletion strain, and the recombinant protein displays both MFE-2 enzymatic activities in vitro. The resolved crystal structure is the first one for a full-length MFE-2 revealing the assembly of domains, and the data can also be transferred to structure-function studies for other MFE-2 proteins. The structure explains the necessity of dimerization. The lack of substrate channelling is proposed based on both the structural features as well as by the fact that hydration and dehydrogenation activities of MFE-2, if produced as separate enzymes, are equally efficient in catalysis as the full-length MFE-2.
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Peroxisomal multifunctional enzyme type 2 from the fruit fly: dehydrogenase and hydratase act as separate entities as revealed by structure and kinetics.,Haataja TJ, Koski MK, Hiltunen JK, Glumoff T Biochem J. 2011 Feb 14. PMID:21320074<ref>PMID:21320074</ref>
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The line below this paragraph, containing "STRUCTURE_3oml", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_3oml| PDB=3oml | SCENE= }}
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===Structure of full-length peroxisomal multifunctional enzyme type 2 from Drosophila melanogaster===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_21320074}}, adds the Publication Abstract to the page
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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 21320074 is the PubMed ID number.
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</StructureSection>
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{{ABSTRACT_PUBMED_21320074}}
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==About this Structure==
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[[3oml]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OML OCA].
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==Reference==
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<ref group="xtra">PMID:021320074</ref><references group="xtra"/>
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[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
[[Category: Glumoff, T]]
[[Category: Glumoff, T]]

Revision as of 10:42, 28 May 2014

Structure of full-length peroxisomal multifunctional enzyme type 2 from Drosophila melanogaster

3oml, resolution 2.15Å

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