4ooz

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of beta-1,4-D-mannanase from Cryptopygus antarcticus in complex with mannopentaose

Structural highlights

4ooz is a 2 chain structure with sequence from Cryptopygus antarcticus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.6Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MANA_CRYAT Hydrolyzes 1,4-beta linked polysaccharide backbones of mannans. Has high activity toward locust bean gum (PubMed:18579426, PubMed:25082572). Also active toward konjac and beta-1,4-mannan. Hydrolyzes mannotetraose (M4) and mannopentaose (M5) to mannobiose (M2) and mannotriose (M3) with a little production of mannose (M1). Hydrolyzes beta-1,4-mannan to M2, M3 and M4. Hardly hydrolyzes M2 and M3. Does not hydrolyze p-nitrophenyl-beta-D-mannopyranoside, gua-gum, carboxymethyl cellulose, soluble starch or laminarin (PubMed:18579426).^[1] ^[2]

Publication Abstract from PubMed

Endo-beta-1,4-d-mannanase from the Antarctic springtail, Cryptopygus antarcticus (CaMan), is a cold-adapted beta-mannanase that has the lowest optimum temperature (30 degrees C) of all known beta-mannanases. Here, we report the apo- and mannopentaose (M5) complex structures of CaMan. Structural comparison of CaMan with other beta-mannanases from the multicellular animals reveals that CaMan has an extended loop that alters topography of the active site. Structural and mutational analyses suggest that this extended loop is linked to the cold-adapted enzymatic activity. From the CaMan-M5 complex structure, we defined the mannose-recognition subsites and observed unreported M5 binding site on the surface of CaMan. Proteins 2014; 82:3217-3223. (c) 2014 Wiley Periodicals, Inc.

Structure-based investigation into the functional roles of the extended loop and substrate-recognition sites in an endo-beta-1,4-d-mannanase from the Antarctic springtail, Cryptopygus antarcticus.,Kim MK, An YJ, Song JM, Jeong CS, Kang MH, Kwon KK, Lee YH, Cha SS Proteins. 2014 Nov;82(11):3217-23. doi: 10.1002/prot.24655. Epub 2014 Aug 19. PMID:25082572^[3]

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

References

↑ Song JM, Nam KW, Kang SG, Kim CG, Kwon ST, Lee YH. Molecular cloning and characterization of a novel cold-active beta-1,4-D-mannanase from the Antarctic springtail, Cryptopygus antarcticus. Comp Biochem Physiol B Biochem Mol Biol. 2008 Sep;151(1):32-40. doi: , 10.1016/j.cbpb.2008.05.005. Epub 2008 May 18. PMID:18579426 doi:http://dx.doi.org/10.1016/j.cbpb.2008.05.005
↑ Kim MK, An YJ, Song JM, Jeong CS, Kang MH, Kwon KK, Lee YH, Cha SS. Structure-based investigation into the functional roles of the extended loop and substrate-recognition sites in an endo-beta-1,4-d-mannanase from the Antarctic springtail, Cryptopygus antarcticus. Proteins. 2014 Nov;82(11):3217-23. doi: 10.1002/prot.24655. Epub 2014 Aug 19. PMID:25082572 doi:http://dx.doi.org/10.1002/prot.24655
↑ Kim MK, An YJ, Song JM, Jeong CS, Kang MH, Kwon KK, Lee YH, Cha SS. Structure-based investigation into the functional roles of the extended loop and substrate-recognition sites in an endo-beta-1,4-d-mannanase from the Antarctic springtail, Cryptopygus antarcticus. Proteins. 2014 Nov;82(11):3217-23. doi: 10.1002/prot.24655. Epub 2014 Aug 19. PMID:25082572 doi:http://dx.doi.org/10.1002/prot.24655

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/4ooz"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4ooz is ON HOLD
+==Crystal structure of beta-1,4-D-mannanase from Cryptopygus antarcticus in complex with mannopentaose==
+<StructureSection load='4ooz' size='340' side='right'caption='[[4ooz]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4ooz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cryptopygus_antarcticus Cryptopygus antarcticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OOZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OOZ FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</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=4ooz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ooz OCA], [https://pdbe.org/4ooz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ooz RCSB], [https://www.ebi.ac.uk/pdbsum/4ooz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ooz ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MANA_CRYAT MANA_CRYAT] Hydrolyzes 1,4-beta linked polysaccharide backbones of mannans. Has high activity toward locust bean gum (PubMed:18579426, PubMed:25082572). Also active toward konjac and beta-1,4-mannan. Hydrolyzes mannotetraose (M4) and mannopentaose (M5) to mannobiose (M2) and mannotriose (M3) with a little production of mannose (M1). Hydrolyzes beta-1,4-mannan to M2, M3 and M4. Hardly hydrolyzes M2 and M3. Does not hydrolyze p-nitrophenyl-beta-D-mannopyranoside, gua-gum, carboxymethyl cellulose, soluble starch or laminarin (PubMed:18579426).<ref>PMID:18579426</ref> <ref>PMID:25082572</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Endo-beta-1,4-d-mannanase from the Antarctic springtail, Cryptopygus antarcticus (CaMan), is a cold-adapted beta-mannanase that has the lowest optimum temperature (30 degrees C) of all known beta-mannanases. Here, we report the apo- and mannopentaose (M5) complex structures of CaMan. Structural comparison of CaMan with other beta-mannanases from the multicellular animals reveals that CaMan has an extended loop that alters topography of the active site. Structural and mutational analyses suggest that this extended loop is linked to the cold-adapted enzymatic activity. From the CaMan-M5 complex structure, we defined the mannose-recognition subsites and observed unreported M5 binding site on the surface of CaMan. Proteins 2014; 82:3217-3223. (c) 2014 Wiley Periodicals, Inc.
-Authors: Kim, M.-K., An, Y.J., Jeong, C.-S., Cha, S.-S.
+Structure-based investigation into the functional roles of the extended loop and substrate-recognition sites in an endo-beta-1,4-d-mannanase from the Antarctic springtail, Cryptopygus antarcticus.,Kim MK, An YJ, Song JM, Jeong CS, Kang MH, Kwon KK, Lee YH, Cha SS Proteins. 2014 Nov;82(11):3217-23. doi: 10.1002/prot.24655. Epub 2014 Aug 19. PMID:25082572<ref>PMID:25082572</ref>
-Description: Crystal structure of beta-1,4-D-mannanase from Cryptopygus antarcticus in complex with mannopentaose
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4ooz" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Cryptopygus antarcticus]]
+[[Category: Large Structures]]
+[[Category: An YJ]]
+[[Category: Cha S-S]]
+[[Category: Jeong C-S]]
+[[Category: Kim M-K]]

4ooz

From Proteopedia

Current revision

Crystal structure of beta-1,4-D-mannanase from Cryptopygus antarcticus in complex with mannopentaose

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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