3a71
From Proteopedia
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==High resolution structure of Penicillium chrysogenum alpha-L-arabinanase== | ==High resolution structure of Penicillium chrysogenum alpha-L-arabinanase== | ||
- | <StructureSection load='3a71' size='340' side='right' caption='[[3a71]], [[Resolution|resolution]] 1.14Å' scene=''> | + | <StructureSection load='3a71' size='340' side='right'caption='[[3a71]], [[Resolution|resolution]] 1.14Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3a71]] is a 1 chain structure with sequence from [ | + | <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> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.14Å</td></tr> |
- | <tr id=' | + | <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> |
- | + | <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> | |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
+ | == Function == | ||
+ | [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]] | ||
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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> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 3a71" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
- | *[[Arabinanase|Arabinanase]] | + | *[[Arabinanase 3D structures|Arabinanase 3D structures]] |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: | + | [[Category: Penicillium chrysogenum]] |
- | [[Category: Sogabe | + | [[Category: Sogabe Y]] |
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Current revision
High resolution structure of Penicillium chrysogenum alpha-L-arabinanase
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