1ogm: Difference between revisions

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[[Image:1ogm.gif|left|200px]]


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==Dex49A from Penicillium minioluteum==
The line below this paragraph, containing "STRUCTURE_1ogm", creates the "Structure Box" on the page.
<StructureSection load='1ogm' size='340' side='right'caption='[[1ogm]], [[Resolution|resolution]] 1.80&Aring;' 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'>[[1ogm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Talaromyces_minioluteus Talaromyces minioluteus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OGM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OGM FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#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=1ogm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ogm OCA], [https://pdbe.org/1ogm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ogm RCSB], [https://www.ebi.ac.uk/pdbsum/1ogm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ogm ProSAT]</span></td></tr>
{{STRUCTURE_1ogm| PDB=1ogm  | SCENE= }}
</table>
 
== Function ==
'''DEX49A FROM PENICILLIUM MINIOLUTEUM'''
[https://www.uniprot.org/uniprot/DEXT_TALMI DEXT_TALMI]
 
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
==Overview==
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/og/1ogm_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ogm ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Dextranase catalyzes the hydrolysis of the alpha-1,6-glycosidic linkage in dextran polymers. The structure of dextranase, Dex49A, from Penicillium minioluteum was solved in the apo-enzyme and product-bound forms. The main domain of the enzyme is a right-handed parallel beta helix, which is connected to a beta sandwich domain at the N terminus. In the structure of the product complex, isomaltose was found to bind in a crevice on the surface of the enzyme. The glycosidic oxygen of the glucose unit in subsite +1 forms a hydrogen bond to the suggested catalytic acid, Asp395. By NMR spectroscopy the reaction course was shown to occur with net inversion at the anomeric carbon, implying a single displacement mechanism. Both Asp376 and Asp396 are suitably positioned to activate the water molecule that performs the nucleophilic attack. A new clan that links glycoside hydrolase families 28 and 49 is suggested.
Dextranase catalyzes the hydrolysis of the alpha-1,6-glycosidic linkage in dextran polymers. The structure of dextranase, Dex49A, from Penicillium minioluteum was solved in the apo-enzyme and product-bound forms. The main domain of the enzyme is a right-handed parallel beta helix, which is connected to a beta sandwich domain at the N terminus. In the structure of the product complex, isomaltose was found to bind in a crevice on the surface of the enzyme. The glycosidic oxygen of the glucose unit in subsite +1 forms a hydrogen bond to the suggested catalytic acid, Asp395. By NMR spectroscopy the reaction course was shown to occur with net inversion at the anomeric carbon, implying a single displacement mechanism. Both Asp376 and Asp396 are suitably positioned to activate the water molecule that performs the nucleophilic attack. A new clan that links glycoside hydrolase families 28 and 49 is suggested.


==About this Structure==
Dextranase from Penicillium minioluteum: reaction course, crystal structure, and product complex.,Larsson AM, Andersson R, Stahlberg J, Kenne L, Jones TA Structure. 2003 Sep;11(9):1111-21. PMID:12962629<ref>PMID:12962629</ref>
1OGM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Penicillium_minioluteum Penicillium minioluteum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OGM OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Dextranase from Penicillium minioluteum: reaction course, crystal structure, and product complex., Larsson AM, Andersson R, Stahlberg J, Kenne L, Jones TA, Structure. 2003 Sep;11(9):1111-21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12962629 12962629]
</div>
[[Category: Dextranase]]
<div class="pdbe-citations 1ogm" style="background-color:#fffaf0;"></div>
[[Category: Penicillium minioluteum]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Jones, T A.]]
__TOC__
[[Category: Larsson, A M.]]
</StructureSection>
[[Category: Stahlberg, J.]]
[[Category: Large Structures]]
[[Category: Dextran degradation]]
[[Category: Talaromyces minioluteus]]
[[Category: Glycosidase]]
[[Category: Jones TA]]
[[Category: Hydrolase]]
[[Category: Larsson AM]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 03:49:14 2008''
[[Category: Stahlberg J]]
Retrieved from "https://proteopedia.org/1ogm"