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1pz2

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Revision as of 15:04, 12 October 2017

Crystal structure of a transient covalent reaction intermediate of a family 51 alpha-L-arabinofuranosidase

Structural highlights

1pz2 is a 2 chain structure with sequence from Atcc 12980. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1pz3, 1qw8, 1qw9
Gene:	ABFA (ATCC 12980)
Activity:	Non-reducing end alpha-L-arabinofuranosidase, with EC number 3.2.1.55
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[IABF_GEOSE] Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the cleavage of terminal alpha-(1->5)-arabinofuranosyl bonds in different hemicellulosic homopolysaccharides (branched and debranched arabinans). It acts preferentially on aryl-alpha-L-arabinofuranosides, and is much less effective on aryl-beta-D-xylopyranosides.^[1] ^[2] ^[3] ^[4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

High-resolution crystal structures of alpha-L-arabinofuranosidase from Geobacillus stearothermophilus T-6, a family 51 glycosidase, are described. The enzyme is a hexamer, and each monomer is organized into two domains: a (beta/alpha)8-barrel and a 12-stranded beta sandwich with jelly-roll topology. The structures of the Michaelis complexes with natural and synthetic substrates, and of the transient covalent arabinofuranosyl-enzyme intermediate represent two stable states in the double displacement mechanism, and allow thorough examination of the catalytic mechanism. The arabinofuranose sugar is tightly bound and distorted by an extensive network of hydrogen bonds. The two catalytic residues are 4.7 A apart, and together with other conserved residues contribute to the stabilization of the oxocarbenium ion-like transition state via charge delocalization and specific protein-substrate interactions. The enzyme is an anti-protonator, and a 1.7 A electrophilic migration of the anomeric carbon takes place during the hydrolysis.

Crystal structure and snapshots along the reaction pathway of a family 51 alpha-L-arabinofuranosidase.,Hovel K, Shallom D, Niefind K, Belakhov V, Shoham G, Baasov T, Shoham Y, Schomburg D EMBO J. 2003 Oct 1;22(19):4922-32. PMID:14517232^[5]

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

References

↑ Shallom D, Belakhov V, Solomon D, Gilead-Gropper S, Baasov T, Shoham G, Shoham Y. The identification of the acid-base catalyst of alpha-arabinofuranosidase from Geobacillus stearothermophilus T-6, a family 51 glycoside hydrolase. FEBS Lett. 2002 Mar 13;514(2-3):163-7. PMID:11943144
↑ Shallom D, Belakhov V, Solomon D, Shoham G, Baasov T, Shoham Y. Detailed kinetic analysis and identification of the nucleophile in alpha-L-arabinofuranosidase from Geobacillus stearothermophilus T-6, a family 51 glycoside hydrolase. J Biol Chem. 2002 Nov 15;277(46):43667-73. Epub 2002 Sep 6. PMID:12221104 doi:http://dx.doi.org/10.1074/jbc.M208285200
↑ Hovel K, Shallom D, Niefind K, Belakhov V, Shoham G, Baasov T, Shoham Y, Schomburg D. Crystal structure and snapshots along the reaction pathway of a family 51 alpha-L-arabinofuranosidase. EMBO J. 2003 Oct 1;22(19):4922-32. PMID:14517232 doi:10.1093/emboj/cdg494
↑ Gilead S, Shoham Y. Purification and characterization of alpha-L-arabinofuranosidase from Bacillus stearothermophilus T-6. Appl Environ Microbiol. 1995 Jan;61(1):170-4. PMID:7887599
↑ Hovel K, Shallom D, Niefind K, Belakhov V, Shoham G, Baasov T, Shoham Y, Schomburg D. Crystal structure and snapshots along the reaction pathway of a family 51 alpha-L-arabinofuranosidase. EMBO J. 2003 Oct 1;22(19):4922-32. PMID:14517232 doi:10.1093/emboj/cdg494

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1pz2"

@@ Line 1: / Line 1: @@
 ==Crystal structure of a transient covalent reaction intermediate of a family 51 alpha-L-arabinofuranosidase==
 <StructureSection load='1pz2' size='340' side='right' caption='[[1pz2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ABFA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 ATCC 12980])</td></tr>
 <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>
-<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=1pz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pz2 OCA], [http://pdbe.org/1pz2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pz2 RCSB], [http://www.ebi.ac.uk/pdbsum/1pz2 PDBsum]</span></td></tr>
+<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=1pz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pz2 OCA], [http://pdbe.org/1pz2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pz2 RCSB], [http://www.ebi.ac.uk/pdbsum/1pz2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pz2 ProSAT]</span></td></tr>
 </table>
 == Function ==

1pz2

From Proteopedia

Revision as of 15:04, 12 October 2017

Crystal structure of a transient covalent reaction intermediate of a family 51 alpha-L-arabinofuranosidase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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