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3a71

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==High resolution structure of Penicillium chrysogenum alpha-L-arabinanase==
==High resolution structure of Penicillium chrysogenum alpha-L-arabinanase==
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<StructureSection load='3a71' size='340' side='right' caption='[[3a71]], [[Resolution|resolution]] 1.14&Aring;' scene=''>
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<StructureSection load='3a71' size='340' side='right'caption='[[3a71]], [[Resolution|resolution]] 1.14&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3a71]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_306.48 Cbs 306.48]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A71 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3A71 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3a71]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Penicillium_chrysogenum Penicillium chrysogenum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A71 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A71 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.14&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3a72|3a72]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-reducing_end_alpha-L-arabinofuranosidase Non-reducing end alpha-L-arabinofuranosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.55 3.2.1.55] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3a71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a71 OCA], [https://pdbe.org/3a71 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a71 RCSB], [https://www.ebi.ac.uk/pdbsum/3a71 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a71 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3a71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a71 OCA], [http://pdbe.org/3a71 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a71 RCSB], [http://www.ebi.ac.uk/pdbsum/3a71 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3a71 ProSAT]</span></td></tr>
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</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q7ZA77_PENCH Q7ZA77_PENCH]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a7/3a71_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a7/3a71_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
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</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=3a71 ConSurf].
</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=3a71 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Arabinanase Abnx from Penicillium chrysogenum 31B, which belongs to the GH93 family, releases arabinobiose from the nonreducing terminus of alpha-1,5-L-arabinan, which is distributed in the primary cell walls of higher plants. Crystal structures of Abnx and of its complex with arabinobiose were determined at the high resolutions of 1.14 A to an R(work) of 10.7% (R(free) = 12.8%) and 1.04 A to an R(work) of 10.4% (R(free) = 12.5%). Abnx has a six-bladed beta-propeller fold with a typical ring-closure mode called `Velcro', in which the last four-stranded beta-sheet is completed by the incorporation of a strand from the N-terminus. Catalytic residues which act as a nucleophile and an acid/base were proposed from the structures and confirmed by site-directed mutagenesis. The substrate-binding groove is enclosed at one end by two residues, Glu64 and Tyr66, which contribute to the recognition of the nonreducing chain end of the polysaccharide. A comparison with the related enzyme Arb93A which has a quite similar overall structure suggested that Abnx has different mechanisms to funnel substrates to the active site and/or to stabilize the transition state.
 
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High-resolution structure of exo-arabinanase from Penicillium chrysogenum.,Sogabe Y, Kitatani T, Yamaguchi A, Kinoshita T, Adachi H, Takano K, Inoue T, Mori Y, Matsumura H, Sakamoto T, Tada T Acta Crystallogr D Biol Crystallogr. 2011 May;67(Pt 5):415-22. Epub 2011, Apr 13. PMID:21543843<ref>PMID:21543843</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 3a71" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
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*[[Arabinanase|Arabinanase]]
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*[[Arabinanase 3D structures|Arabinanase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cbs 306 48]]
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[[Category: Large Structures]]
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[[Category: Non-reducing end alpha-L-arabinofuranosidase]]
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[[Category: Penicillium chrysogenum]]
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[[Category: Sogabe, Y]]
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[[Category: Sogabe Y]]
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[[Category: Arabinase]]
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[[Category: Glycosyl hydrolase]]
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[[Category: Hydrolase]]
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Current revision

High resolution structure of Penicillium chrysogenum alpha-L-arabinanase

PDB ID 3a71

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