1JG5

CRYSTAL STRUCTURE OF RAT GTP CYCLOHYDROLASE I FEEDBACK REGULATORY PROTEIN, GFRP

PDB DOI: https://doi.org/10.2210/pdb1JG5/pdb

Classification: PROTEIN BINDING
Organism(s): Rattus norvegicus
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2001-06-23 Released: 2001-10-10
Deposition Author(s): Bader, G., Schiffmann, S., Herrmann, A., Fischer, M., Gutlich, M., Auerbach, G., Ploom, T., Bacher, A., Huber, R., Lemm, T.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.60 Å
R-Value Free: 0.214
R-Value Work: 0.166

wwPDB Validation 3D Report Full Report

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

Literature

Crystal structure of rat GTP cyclohydrolase I feedback regulatory protein, GFRP.

Bader, G., Schiffmann, S., Herrmann, A., Fischer, M., Gutlich, M., Auerbach, G., Ploom, T., Bacher, A., Huber, R., Lemm, T.

(2001) J Mol Biol 312: 1051-1057

PubMed: 11580249 Search on PubMed
DOI: https://doi.org/10.1006/jmbi.2001.5011
Primary Citation of Related Structures:
1JG5

PubMed Abstract:
Tetrahydrobiopterin, the cofactor required for hydroxylation of aromatic amino acids regulates its own synthesis in mammals through feedback inhibition of GTP cyclohydrolase I. This mechanism is mediated by a regulatory subunit called GTP cyclohydrolase I feedback regulatory protein (GFRP). The 2.6 A resolution crystal structure of rat GFRP shows that the protein forms a pentamer. This indicates a model for the interaction of mammalian GTP cyclohydrolase I with its regulator, GFRP. Kinetic investigations of human GTP cyclohydrolase I in complex with rat and human GFRP showed similar regulatory effects of both GFRP proteins.

Organizational Affiliation

Abteilung Strukturforschung, Max-Planck-Institut für Biochemie, Am Klopferspitz 18a, Martinsried, D-82152, Germany.

Macromolecule Content

Total Structure Weight: 47.96 kDa
Atom Count: 3,601
Modelled Residue Count: 415
Deposited Residue Count: 415
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
GTP CYCLOHYDROLASE I FEEDBACK REGULATORY PROTEIN	A, B, C, D, E	83	Rattus norvegicus	Mutation(s): 0
UniProt
Find proteins for P70552 (Rattus norvegicus) Explore P70552 Go to UniProtKB: P70552
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P70552
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
K Query on K Download Ideal Coordinates CCD File SDF format, chain F [auth A] SDF format, chain G [auth B] SDF format, chain H [auth C] SDF format, chain I [auth D] SDF format, chain J [auth E] MOL2 format, chain F [auth A] MOL2 format, chain G [auth B] MOL2 format, chain H [auth C] MOL2 format, chain I [auth D] MOL2 format, chain J [auth E] mmCIF format, chain F [auth A] mmCIF format, chain G [auth B] mmCIF format, chain H [auth C] mmCIF format, chain I [auth D] mmCIF format, chain J [auth E]	F [auth A], G [auth B], H [auth C], I [auth D], J [auth E]	POTASSIUM ION K NPYPAHLBTDXSSS-UHFFFAOYSA-N		Interactions Focus chain F [auth A] Focus chain G [auth B] Focus chain H [auth C] Focus chain I [auth D] Focus chain J [auth E] Interactions & Density Focus chain F [auth A] Focus chain G [auth B] Focus chain H [auth C] Focus chain I [auth D] Focus chain J [auth E]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.60 Å
R-Value Free: 0.214
R-Value Work: 0.166
Space Group: P 2₁ 2₁ 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 106.803	α = 90
b = 110.052	β = 90
c = 38.686	γ = 90

Software Package:

Software Name	Purpose
PROTEIN	model building
CNS	refinement
DENZO	data reduction
SCALEPACK	data scaling
PROTEIN	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2001-10-10

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2001-10-10
Type: Initial release
Version 1.1: 2008-04-27
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2024-03-13
Changes: Data collection, Database references, Derived calculations