5YY3

Crystal structure of AsqI

PDB DOI: https://doi.org/10.2210/pdb5YY3/pdb

Classification: METAL BINDING PROTEIN
Organism(s): Aspergillus nidulans FGSC A4
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2017-12-07 Released: 2018-08-01
Deposition Author(s): Hara, K., Hashimoto, H., Kishimoto, S., Watanabe, K.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.31 Å
R-Value Free: 0.220
R-Value Work: 0.193
R-Value Observed: 0.194

wwPDB Validation 3D Report Full Report

This is version 1.1 of the entry. See complete history.

Literature

Enzymatic one-step ring contraction for quinolone biosynthesis.

Kishimoto, S., Hara, K., Hashimoto, H., Hirayama, Y., Champagne, P.A., Houk, K.N., Tang, Y., Watanabe, K.

(2018) Nat Commun 9: 2826-2826

PubMed: 30026518 Search on PubMedSearch on PubMed Central
DOI: https://doi.org/10.1038/s41467-018-05221-5
Primary Citation of Related Structures:
5YY2, 5YY3

PubMed Abstract:
The 6,6-quinolone scaffolds on which viridicatin-type fungal alkaloids are built are frequently found in metabolites that display useful biological activities. Here we report in vitro and computational analyses leading to the discovery of a hemocyanin-like protein AsqI from the Aspergillus nidulans aspoquinolone biosynthetic pathway that forms viridicatins via a conversion of the cyclopenin-type 6,7-bicyclic system into the viridicatin-type 6,6-bicyclic core through elimination of carbon dioxide and methylamine through methyl isocyanate.

Organizational Affiliation

Department of Pharmaceutical Sciences, University of Shizuoka, Shizuoka, 422-8526, Japan.

Macromolecule Content

Total Structure Weight: 85.64 kDa
Atom Count: 4,943
Modelled Residue Count: 577
Deposited Residue Count: 749
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Uncharacterized protein AsqI	A	749	Aspergillus nidulans FGSC A4	Mutation(s): 0 Gene Names: ANIA_11193
UniProt
Find proteins for C8VJQ3 (Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)) Explore C8VJQ3 Go to UniProtKB: C8VJQ3
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	C8VJQ3
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.31 Å
R-Value Free: 0.220
R-Value Work: 0.193
R-Value Observed: 0.194
Space Group: I 2 2 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 85.082	α = 90
b = 117.435	β = 90
c = 159	γ = 90

Software Package:

Software Name	Purpose
PHENIX	refinement
XDS	data reduction
Aimless	data scaling
PHENIX	phasing
Coot	model building

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2018-08-01

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2018-08-01
Type: Initial release
Version 1.1: 2024-03-27
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.