1SLL

SIALIDASE L FROM LEECH MACROBDELLA DECORA

PDB DOI: https://doi.org/10.2210/pdb1SLL/pdb

Classification: HYDROLASE
Organism(s): Macrobdella decora
Expression System: Escherichia coli BL21(DE3)
Mutation(s): No

Deposited: 1997-10-14 Released: 1998-12-16
Deposition Author(s): Luo, Y., Li, S.C., Chou, M.Y., Li, Y.T., Luo, M.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.00 Å
R-Value Free: 0.224
R-Value Work: 0.167
R-Value Observed: 0.167

wwPDB Validation 3D Report Full Report

This is version 1.3 of the entry. See complete history.

Literature

The crystal structure of an intramolecular trans-sialidase with a NeuAc alpha2-->3Gal specificity.

Luo, Y., Li, S.C., Chou, M.Y., Li, Y.T., Luo, M.

(1998) Structure 6: 521-530

PubMed: 9562562 Search on PubMed
DOI: https://doi.org/10.1016/s0969-2126(98)00053-7
Primary Citation of Related Structures:
1SLI, 1SLL

PubMed Abstract:
Intramolecular trans-sialidase from leech (Macrobdella decora) is a unique enzyme which cleaves the terminal neuraminic acid (NeuAc) residue from sialoglycoconjugates, releasing 2, 7-anhydro-neuraminic acid (2,7-anhydro-NeuAc). It is the first enzyme found to exhibit strictly specific cleavage of NeuAc alpha2-->3Gal linkages in sialoglycoconjugates. The release of 2,7-anhydro-NeuAc instead of NeuAc implies a unique mechanism, in which the sialosyl linkage is transferred within the sialoglycoconjugate rather than hydrolyzed. The aims of the structural study were to gain structural insight into the strict specificity and unique mechanism of this unusual enzyme.

Organizational Affiliation

Center for Macromolecular Crystallography, University of Alabama at Birmingham, Alabama 35294, USA.

Macromolecule Content

Total Structure Weight: 74.57 kDa
Atom Count: 5,938
Modelled Residue Count: 679
Deposited Residue Count: 679
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
SIALIDASE L	A	679	Macrobdella decora	Mutation(s): 0 Gene Names: T7 EC: 3.2.1.18
UniProt
Find proteins for Q27701 (Macrobdella decora) Explore Q27701 Go to UniProtKB: Q27701
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q27701
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.00 Å
R-Value Free: 0.224
R-Value Work: 0.167
R-Value Observed: 0.167
Space Group: P 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 46.364	α = 113.48
b = 69.275	β = 95.41
c = 72.469	γ = 107.31

Software Package:

Software Name	Purpose
MLPHARE	phasing
X-PLOR	refinement
DENZO	data reduction
SCALEPACK	data scaling

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 1998-12-16

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 1998-12-16
Type: Initial release
Version 1.1: 2008-03-24
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2024-02-14
Changes: Data collection, Database references

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.