1ogo: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
New page: left|200px<br /> <applet load="1ogo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ogo, resolution 1.65Å" /> '''DEX49A FROM PENICIL...
 
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
 
(23 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1ogo.gif|left|200px]]<br />
<applet load="1ogo" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ogo, resolution 1.65&Aring;" />
'''DEX49A FROM PENICILLIUM MINIOLUTEUM COMPLEX WITH ISOMALTOSE'''<br />


==Overview==
==Dex49A from Penicillium minioluteum complex with isomaltose==
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, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?12962629 (full description)]]
<StructureSection load='1ogo' size='340' side='right'caption='[[1ogo]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ogo]] 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=1OGO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OGO 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]] 1.65&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene></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=1ogo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ogo OCA], [https://pdbe.org/1ogo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ogo RCSB], [https://www.ebi.ac.uk/pdbsum/1ogo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ogo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DEXT_TALMI DEXT_TALMI]
== 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/og/1ogo_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=1ogo 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.


==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>
1OGO is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Penicillium_minioluteum Penicillium minioluteum]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.11 3.2.1.11]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OGO 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12962629 12962629]
</div>
[[Category: Penicillium minioluteum]]
<div class="pdbe-citations 1ogo" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
== References ==
[[Category: Jones, T.A.]]
<references/>
[[Category: Larsson, A.M.]]
__TOC__
[[Category: Stahlberg, J.]]
</StructureSection>
[[Category: dextran degradation]]
[[Category: Large Structures]]
[[Category: glycosidase]]
[[Category: Talaromyces minioluteus]]
[[Category: hydrolase]]
[[Category: Jones TA]]
 
[[Category: Larsson AM]]
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 21:15:23 2007''
[[Category: Stahlberg J]]
Retrieved from "https://proteopedia.org/1ogo"