5E9O

Spirochaeta thermophila X module - CBM64 - mutant G504A

PDB DOI: https://doi.org/10.2210/pdb5E9O/pdb

Classification: HYDROLASE
Organism(s): Spirochaeta thermophila
Expression System: Escherichia coli BL21(DE3)
Mutation(s): Yes

Deposited: 2015-10-15 Released: 2016-03-02
Deposition Author(s): Schiefner, A., Skerra, A.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.10 Å
R-Value Free: 0.219
R-Value Work: 0.179
R-Value Observed: 0.181

wwPDB Validation 3D Report Full Report

Ligand Structure Quality Assessment

This is version 1.2 of the entry. See complete history.

Literature

Structural basis for cellulose binding by the type A carbohydrate-binding module 64 of Spirochaeta thermophila.

Schiefner, A., Angelov, A., Liebl, W., Skerra, A.

(2016) Proteins 84: 855-858

PubMed: 26868291 Search on PubMed
DOI: https://doi.org/10.1002/prot.25010
Primary Citation of Related Structures:
5E9O, 5E9P

PubMed Abstract:
Spirochaeta thermophila secretes seven glycoside hydrolases for plant biomass degradation that carry a carbohydrate-binding module 64 (CBM64) appended at the C-terminus. CBM64 adsorbs to various β1-4-linked pyranose substrates and shows high affinity for cellulose. We present the first crystal structure of a CBM64 at 1.2 Å resolution, which reveals a jelly-roll-like fold corresponding to a surface-binding type A CBM. Modeling of its interaction with cellulose indicates that CBM64 achieves association with the hydrophobic face of β-linked pyranose chains via a unique coplanar arrangement of four exposed tryptophan side chains. Proteins 2016; 84:855-858. © 2016 Wiley Periodicals, Inc.

Organizational Affiliation

Munich Center for Integrated Protein Science (CIPS-M) and Lehrstuhl für Biologische Chemie, Technische Universität München, 85354 Freising (Weihenstephan), Germany.

Macromolecule Content

Total Structure Weight: 42.95 kDa
Atom Count: 3,103
Modelled Residue Count: 340
Deposited Residue Count: 344
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Cellulase, glycosyl hydrolase family 5, TPS linker, domain X	A, B, C, D	86	Spirochaeta thermophila	Mutation(s): 1 Gene Names: STHERM_c20620
UniProt
Find proteins for E0RQU0 (Spirochaeta thermophila (strain ATCC 49972 / DSM 6192 / RI 19.B1)) Explore E0RQU0 Go to UniProtKB: E0RQU0
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	E0RQU0
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
I3C Query on I3C Download Ideal Coordinates CCD File SDF format, chain E [auth B] SDF format, chain F [auth C] SDF format, chain G [auth C] SDF format, chain H [auth D] SDF format, chain I [auth D] MOL2 format, chain E [auth B] MOL2 format, chain F [auth C] MOL2 format, chain G [auth C] MOL2 format, chain H [auth D] MOL2 format, chain I [auth D]	E [auth B], F [auth C], G [auth C], H [auth D], I [auth D]	5-amino-2,4,6-triiodobenzene-1,3-dicarboxylic acid C₈ H₄ I₃ N O₄ JEZJSNULLBSYHV-UHFFFAOYSA-N		Interactions Focus chain E [auth B] Focus chain F [auth C] Focus chain G [auth C] Focus chain H [auth D] Focus chain I [auth D] Interactions & Density Focus chain E [auth B] Focus chain F [auth C] Focus chain G [auth C] Focus chain H [auth D] Focus chain I [auth D]