1sdg: Difference between revisions

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{{Theoretical_model}}
{{Theoretical_model}}
{{Seed}}
[[Image:1sdg.png|left|200px]]


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==MOLECULAR ASPECTS OF FUNCTIONAL DIFFERENCES BETWEEN ALCOHOL AND SORBITOL DEHYDROGENASES==
The line below this paragraph, containing "STRUCTURE_1sdg", creates the "Structure Box" on the page.
<StructureSection load='1sdg' size='340' side='right'caption='[[1sdg]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SDG FirstGlance]. <br>
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</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=1sdg FirstGlance], [https://www.ebi.ac.uk/pdbsum/1sdg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sdg ProSAT]</span></td></tr>
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</table>
{{STRUCTURE_1sdg|  PDB=1sdg  |  SCENE=  }}
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The amino acid sequence of sheep liver sorbitol dehydrogenase has been fitted to the high-resolution model of the homologous horse liver alcohol dehydrogenase by computer graphics. This has allowed construction of a model of sorbitol dehydrogenase that provides explanations why sorbitol is not a substrate for alcohol dehydrogenase, why ethanol is not a substrate for sorbitol dehydrogenase, and what determines its specificity for polyols. An important feature of the model is that one of the ligands to the active site zinc atom is a glutamic acid residue instead of a cysteine residue, which is the corresponding ligand in the homologous alcohol dehydrogenases. This is one component of the structural change that can be related to the different substrate specificities, showing how altered enzymic activity might be brought about by structural changes of the kind that it is now possible to introduce by site-directed mutagenesis and recombinant DNA techniques.


===MOLECULAR ASPECTS OF FUNCTIONAL DIFFERENCES BETWEEN ALCOHOL AND SORBITOL DEHYDROGENASES===
Molecular aspects of functional differences between alcohol and sorbitol dehydrogenases.,Eklund H, Horjales E, Jornvall H, Branden CI, Jeffery J Biochemistry. 1985 Dec 31;24(27):8005-12. PMID:2936393<ref>PMID:2936393</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1sdg" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 2936393 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_2936393}}
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</StructureSection>
==About this Structure==
[[Category: Theoretical Model]]
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SDG OCA].
[[Category: Large Structures]]
 
==Reference==
<ref group="xtra">PMID:2936393</ref><references group="xtra"/>
[[Category: Branden, C.-I]]
[[Category: Branden, C.-I]]
[[Category: Eklund, H]]
[[Category: Eklund, H]]
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[[Category: Jeffery, J]]
[[Category: Jeffery, J]]
[[Category: Jornvall, H]]
[[Category: Jornvall, H]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr  8 07:05:16 2010''

Latest revision as of 10:29, 22 September 2021

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

MOLECULAR ASPECTS OF FUNCTIONAL DIFFERENCES BETWEEN ALCOHOL AND SORBITOL DEHYDROGENASESMOLECULAR ASPECTS OF FUNCTIONAL DIFFERENCES BETWEEN ALCOHOL AND SORBITOL DEHYDROGENASES

Structural highlights

For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, PDBsum, ProSAT

Publication Abstract from PubMed

The amino acid sequence of sheep liver sorbitol dehydrogenase has been fitted to the high-resolution model of the homologous horse liver alcohol dehydrogenase by computer graphics. This has allowed construction of a model of sorbitol dehydrogenase that provides explanations why sorbitol is not a substrate for alcohol dehydrogenase, why ethanol is not a substrate for sorbitol dehydrogenase, and what determines its specificity for polyols. An important feature of the model is that one of the ligands to the active site zinc atom is a glutamic acid residue instead of a cysteine residue, which is the corresponding ligand in the homologous alcohol dehydrogenases. This is one component of the structural change that can be related to the different substrate specificities, showing how altered enzymic activity might be brought about by structural changes of the kind that it is now possible to introduce by site-directed mutagenesis and recombinant DNA techniques.

Molecular aspects of functional differences between alcohol and sorbitol dehydrogenases.,Eklund H, Horjales E, Jornvall H, Branden CI, Jeffery J Biochemistry. 1985 Dec 31;24(27):8005-12. PMID:2936393[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Eklund H, Horjales E, Jornvall H, Branden CI, Jeffery J. Molecular aspects of functional differences between alcohol and sorbitol dehydrogenases. Biochemistry. 1985 Dec 31;24(27):8005-12. PMID:2936393
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