2cov

From Proteopedia

(Difference between revisions)

Revision as of 10:26, 6 September 2023

Crystal structure of CBM31 from beta-1,3-xylanase

Structural highlights

2cov is a 6 chain structure with sequence from Alcaligenes sp. XY-234. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.25Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

3XYN_ALCSP Catalyzes the hydrolysis of beta-1,3-xylan into oligosaccharides, mainly xylotriose and xylobiose with smaller amounts of xylotetraose, xylose, xylopentaose and xylohexaose. Does not hydrolyze xylobiose, p-nitrophenyl-beta-xyloside, beta-1,4-xylan, carboxymethylcellulose, curdlan, glucomannan or beta-1,4-mannan.^[1] ^[2]

Publication Abstract from PubMed

Here, we present the crystal structure of the family 31 carbohydrate-binding module (CBM) of beta-1,3-xylanase from Alcaligenes sp. strain XY-234 (AlcCBM31) determined at a resolution of 1.25A. The AlcCBM31 shows affinity with only beta-1,3-xylan. The AlcCBM31 molecule makes a beta-sandwich structure composed of eight beta-strands with a typical immunoglobulin fold and contains two intra-molecular disulfide bonds. The folding topology of AlcCBM31 differs from that of the large majority of other CBMs, in which eight beta-strands comprise a beta-sandwich structure with a typical jelly-roll fold. AlcCBM31 shows structural similarity with CBM structures of family 34 and family 9, which also adopt structures based on immunoglobulin folds.

The first crystal structure of a family 31 carbohydrate-binding module with affinity to beta-1,3-xylan.,Hashimoto H, Tamai Y, Okazaki F, Tamaru Y, Shimizu T, Araki T, Sato M FEBS Lett. 2005 Aug 15;579(20):4324-8. PMID:16061225^[3]

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

References

↑ Okazaki F, Tamaru Y, Hashikawa S, Li YT, Araki T. Novel carbohydrate-binding module of beta-1,3-xylanase from a marine bacterium, Alcaligenes sp. strain XY-234. J Bacteriol. 2002 May;184(9):2399-403. PMID:11948152
↑ Araki T, Inoue N, Morishita T. Purification and characterization of beta-1,3-xylanase from a marine bacterium, Alcaligenes sp. XY-234. J Gen Appl Microbiol. 1998 Aug;44(4):269-274. PMID:12501421
↑ Hashimoto H, Tamai Y, Okazaki F, Tamaru Y, Shimizu T, Araki T, Sato M. The first crystal structure of a family 31 carbohydrate-binding module with affinity to beta-1,3-xylan. FEBS Lett. 2005 Aug 15;579(20):4324-8. PMID:16061225 doi:http://dx.doi.org/S0014-5793(05)00820-3

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2cov"

@@ Line 3: / Line 3: @@
 <StructureSection load='2cov' size='340' side='right'caption='[[2cov]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2cov]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Alcaligenes_sp._xy-234 Alcaligenes sp. xy-234]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2COV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2COV FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2cov]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Alcaligenes_sp._XY-234 Alcaligenes sp. XY-234]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2COV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2COV FirstGlance]. <br>
-</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=2cov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cov OCA], [https://pdbe.org/2cov PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cov RCSB], [https://www.ebi.ac.uk/pdbsum/2cov PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cov ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.25&#8491;</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=2cov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cov OCA], [https://pdbe.org/2cov PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cov RCSB], [https://www.ebi.ac.uk/pdbsum/2cov PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cov ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/3XYN_ALCSP 3XYN_ALCSP]] Catalyzes the hydrolysis of beta-1,3-xylan into oligosaccharides, mainly xylotriose and xylobiose with smaller amounts of xylotetraose, xylose, xylopentaose and xylohexaose. Does not hydrolyze xylobiose, p-nitrophenyl-beta-xyloside, beta-1,4-xylan, carboxymethylcellulose, curdlan, glucomannan or beta-1,4-mannan.<ref>PMID:11948152</ref> <ref>PMID:12501421</ref>
+[https://www.uniprot.org/uniprot/3XYN_ALCSP 3XYN_ALCSP] Catalyzes the hydrolysis of beta-1,3-xylan into oligosaccharides, mainly xylotriose and xylobiose with smaller amounts of xylotetraose, xylose, xylopentaose and xylohexaose. Does not hydrolyze xylobiose, p-nitrophenyl-beta-xyloside, beta-1,4-xylan, carboxymethylcellulose, curdlan, glucomannan or beta-1,4-mannan.<ref>PMID:11948152</ref> <ref>PMID:12501421</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Alcaligenes sp. xy-234]]
+[[Category: Alcaligenes sp. XY-234]]
 [[Category: Large Structures]]
-[[Category: Araki, T]]
+[[Category: Araki T]]
-[[Category: Hashimoto, H]]
+[[Category: Hashimoto H]]
-[[Category: Okazaki, F]]
+[[Category: Okazaki F]]
-[[Category: Sato, M]]
+[[Category: Sato M]]
-[[Category: Shimizu, T]]
+[[Category: Shimizu T]]
-[[Category: Tamai, Y]]
+[[Category: Tamai Y]]
-[[Category: Tamaru, Y]]
+[[Category: Tamaru Y]]
-[[Category: 3-xylanase]]
-[[Category: Beta-1]]
-[[Category: Carbohydrate-binding module]]
-[[Category: Family 31 cbm]]
-[[Category: Sugar binding protein]]

2cov

From Proteopedia

Revision as of 10:26, 6 September 2023

Crystal structure of CBM31 from beta-1,3-xylanase

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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