1j9y

From Proteopedia

(Difference between revisions)

Revision as of 03:40, 11 September 2015

Crystal structure of mannanase 26A from Pseudomonas cellulosa

Structural highlights

1j9y is a 1 chain structure with sequence from "cellvibrio_cellulosa"_nagy_et_al._2002 "cellvibrio cellulosa" nagy et al. 2002. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	Man26A ("Cellvibrio cellulosa" Nagy et al. 2002)
Activity:	Mannan endo-1,4-beta-mannosidase, with EC number 3.2.1.78
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[MANA_CELJU] Hydrolyzes mannan and galactomannan, but displays little activity towards other polysaccharides located in the plant cell wall. Appears to act in synergy with alpha-galactosidase (AgaA) to elicit hydrolysis of galactomannan. Preferentially hydrolyzes the larger oligosaccharides and has greater activity against non-substituted polysaccharides.^[1] ^[2]

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

The crystal structure of Pseudomonas cellulosa mannanase 26A has been solved by multiple isomorphous replacement and refined at 1.85 A resolution to an R-factor of 0.182 (R-free = 0.211). The enzyme comprises (beta/alpha)(8)-barrel architecture with two catalytic glutamates at the ends of beta-strands 4 and 7 in precisely the same location as the corresponding glutamates in other 4/7-superfamily glycoside hydrolase enzymes (clan GH-A glycoside hydrolases). The family 26 glycoside hydrolases are therefore members of clan GH-A. Functional analyses of mannanase 26A, informed by the crystal structure of the enzyme, provided important insights into the role of residues close to the catalytic glutamates. These data showed that Trp-360 played a critical role in binding substrate at the -1 subsite, whereas Tyr-285 was important to the function of the nucleophile catalyst. His-211 in mannanase 26A does not have the same function as the equivalent asparagine in the other GH-A enzymes. The data also suggest that Trp-217 and Trp-162 are important for the activity of mannanase 26A against mannooligosaccharides but are less important for activity against polysaccharides.

Crystal structure of mannanase 26A from Pseudomonas cellulosa and analysis of residues involved in substrate binding.,Hogg D, Woo EJ, Bolam DN, McKie VA, Gilbert HJ, Pickersgill RW J Biol Chem. 2001 Aug 17;276(33):31186-92. Epub 2001 May 29. PMID:11382747^[3]

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

References

↑ Braithwaite KL, Black GW, Hazlewood GP, Ali BR, Gilbert HJ. A non-modular endo-beta-1,4-mannanase from Pseudomonas fluorescens subspecies cellulosa. Biochem J. 1995 Feb 1;305 ( Pt 3):1005-10. PMID:7848261
↑ Halstead JR, Fransen MP, Eberhart RY, Park AJ, Gilbert HJ, Hazlewood GP. alpha-Galactosidase A from Pseudomonas fluorescens subsp. cellulosa: cloning, high level expression and its role in galactomannan hydrolysis. FEMS Microbiol Lett. 2000 Nov 15;192(2):197-203. PMID:11064195
↑ Hogg D, Woo EJ, Bolam DN, McKie VA, Gilbert HJ, Pickersgill RW. Crystal structure of mannanase 26A from Pseudomonas cellulosa and analysis of residues involved in substrate binding. J Biol Chem. 2001 Aug 17;276(33):31186-92. Epub 2001 May 29. PMID:11382747 doi:10.1074/jbc.M010290200

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1j9y"

@@ Line 2: / Line 2: @@
 <StructureSection load='1j9y' size='340' side='right' caption='[[1j9y]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1j9y]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cellvibrio_japonicus Cellvibrio japonicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J9Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1J9Y FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1j9y]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"cellvibrio_cellulosa"_nagy_et_al._2002 "cellvibrio cellulosa" nagy et al. 2002]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J9Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1J9Y FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Man26A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=155077 Cellvibrio japonicus])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Man26A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=155077 "Cellvibrio cellulosa" Nagy et al. 2002])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannan_endo-1,4-beta-mannosidase Mannan endo-1,4-beta-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.78 3.2.1.78] </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=1j9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j9y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1j9y RCSB], [http://www.ebi.ac.uk/pdbsum/1j9y 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=1j9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j9y OCA], [http://pdbe.org/1j9y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1j9y RCSB], [http://www.ebi.ac.uk/pdbsum/1j9y PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MANA_PSEFL MANA_PSEFL]] Hydrolyzes mannan and galactomannan, but displays little activity towards other polysaccharides located in the plant cell wall. Appears to act in synergy with alpha-galactosidase (AgaA) to elicit hydrolysis of galactomannan. Preferentially hydrolyzes the larger oligosaccharides and has greater activity against non-substituted polysaccharides.<ref>PMID:7848261</ref> <ref>PMID:11064195</ref>
+[[http://www.uniprot.org/uniprot/MANA_CELJU MANA_CELJU]] Hydrolyzes mannan and galactomannan, but displays little activity towards other polysaccharides located in the plant cell wall. Appears to act in synergy with alpha-galactosidase (AgaA) to elicit hydrolysis of galactomannan. Preferentially hydrolyzes the larger oligosaccharides and has greater activity against non-substituted polysaccharides.<ref>PMID:7848261</ref> <ref>PMID:11064195</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 28: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1j9y" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 35: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Cellvibrio japonicus]]
+[[Category: Cellvibrio cellulosa nagy et al. 2002]]
 [[Category: Mannan endo-1,4-beta-mannosidase]]
 [[Category: Bolam, D N]]

1j9y

From Proteopedia

Revision as of 03:40, 11 September 2015

Crystal structure of mannanase 26A from Pseudomonas cellulosa

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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