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5x37

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Solution structure of the Family 1 carbohydrate-binding module with mannosylated Ser14

Structural highlights

5x37 is a 1 chain structure with sequence from Trichoderma reesei. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GUX1_HYPJE The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.

Publication Abstract from PubMed

Protein glycosylation has been shown to have a variety of site-specific and glycan-specific effects, but so far, the molecular logic that leads to such observations has been elusive. Understanding the structural changes that occur and being able to correlate those with the physical properties of the glycopeptide are valuable steps toward being able to predict how specific glycosylation patterns will affect the stability of glycoproteins. By systematically comparing the structural features of the O-glycosylated carbohydrate-binding module of a Trichoderma reesei-derived Family 7 cellobiohydrolase, we were able to develop a better understanding of the influence of O-glycan structure on the molecule's physical stability. Our results indicate that the previously observed stabilizing effects of O-glycans come from the introduction of new bonding interactions to the structure and increased rigidity, while the decreased stability seemed to result from the impaired interactions and increased conformational flexibility. This type of knowledge provides a powerful and potentially general mechanism for improving the stability of proteins through glycoengineering.

Structural Insight into the Stabilizing Effect of O-Glycosylation.,Chaffey PK, Guan X, Chen C, Ruan Y, Wang X, Tran AH, Koelsch TN, Cui Q, Feng Y, Tan Z Biochemistry. 2017 Jun 13;56(23):2897-2906. doi: 10.1021/acs.biochem.7b00195., Epub 2017 Jun 1. PMID:28494147^[1]

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

References

↑ Chaffey PK, Guan X, Chen C, Ruan Y, Wang X, Tran AH, Koelsch TN, Cui Q, Feng Y, Tan Z. Structural Insight into the Stabilizing Effect of O-Glycosylation. Biochemistry. 2017 Jun 13;56(23):2897-2906. doi: 10.1021/acs.biochem.7b00195., Epub 2017 Jun 1. PMID:28494147 doi:http://dx.doi.org/10.1021/acs.biochem.7b00195

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5x37"

Categories: Large Structures | Trichoderma reesei | Feng Y | Tan Z

@@ Line 1: / Line 1: @@
 ==Solution structure of the Family 1 carbohydrate-binding module with mannosylated Ser14==
-<StructureSection load='5x37' size='340' side='right' caption='[[5x37]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='5x37' size='340' side='right'caption='[[5x37]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5x37]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X37 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5X37 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5x37]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X37 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5X37 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5x34|5x34]], [[5x35|5x35]], [[5x36|5x36]], [[5x38|5x38]], [[5x39|5x39]], [[5x3c|5x3c]]</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=5x37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x37 OCA], [https://pdbe.org/5x37 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5x37 RCSB], [https://www.ebi.ac.uk/pdbsum/5x37 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5x37 ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase_(non-reducing_end) Cellulose 1,4-beta-cellobiosidase (non-reducing end)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] </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=5x37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x37 OCA], [http://pdbe.org/5x37 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x37 RCSB], [http://www.ebi.ac.uk/pdbsum/5x37 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x37 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/GUX1_HYPJE GUX1_HYPJE]] The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
+[https://www.uniprot.org/uniprot/GUX1_HYPJE GUX1_HYPJE] The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 18: @@
 </div>
 <div class="pdbe-citations 5x37" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Cellobiohydrolase 3D structures|Cellobiohydrolase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Feng, Y]]
+[[Category: Large Structures]]
-[[Category: Tan, Z]]
+[[Category: Trichoderma reesei]]
-[[Category: Carbohydrate binding]]
+[[Category: Feng Y]]
-[[Category: Hydrolase]]
+[[Category: Tan Z]]

5x37

From Proteopedia

Current revision

Solution structure of the Family 1 carbohydrate-binding module with mannosylated Ser14

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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