PDBsum entry: 1ll8

Transferase

PDB-id: 1ll8

Contents

Description

Header details

Header records

References

PROCHECK

Protein chain

114 a.a. *

* Residue conservation analysis

Tools

Clefts Calculation

PDB id:

1ll8

Name:

Transferase

Title:

Structure and interactions of pas kinase n-terminal pas domain: model for intramolecular kinase regulation

Structure:

Pas kinase. Chain: a. Fragment: pas-a domain. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

UniProt:

Q96RG2 (PASK_HUMAN)

Seq:

Struc:

Seq:

Struc:

Seq:

Struc:

Seq:

Struc:

Seq:

Struc:

Seq:

1323 a.a.

Struc:

114 a.a.*

Key:	PfamA domain	PfamB domain
Secondary structure	CATH domain

* PDB and UniProt seqs differ at 6 residue positions (black crosses)

Enzyme class:

E.C.2.7.11.1   [IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

Reaction:

ATP + a protein = ADP + a phosphoprotein

Resolution:

not givenÅ

NMR structure:

20 models

Authors:

C.A.Amezcua,S.M.Harper,J.Rutter,K.H.Gardner

Key ref:

C.A.Amezcua et al. (2002). Structure and interactions of PAS kinase N-terminal PAS domain: model for intramolecular kinase regulation.. Structure, 10, 1349-1361. [PubMed id: 12377121] [DOI: 10.1016/S0969-2126(02)00857-2]

Date:

26-Apr-02

Release date:

09-Oct-02

Related entries:

5354 related db: bmrb

Quick_links

Procheck

Clefts

Surface

Key reference

DOI no: 10.1016/S0969-2126(02)00857-2

Structure 10:1349-1361 (2002)

PubMed id: 12377121

Structure and interactions of PAS kinase N-terminal PAS domain: model for intramolecular kinase regulation.

C.A.Amezcua, S.M.Harper, J.Rutter, K.H.Gardner.

ABSTRACT

PAS domains are sensory modules in signal-transducing proteins that control responses to various environmental stimuli. To examine how those domains can regulate a eukaryotic kinase, we have studied the structure and binding interactions of the N-terminal PAS domain of human PAS kinase using solution NMR methods. While this domain adopts a characteristic PAS fold, two regions are unusually flexible in solution. One of these serves as a portal that allows small organic compounds to enter into the core of the domain, while the other binds and inhibits the kinase domain within the same protein. Structural and functional analyses of point mutants demonstrate that the compound and ligand binding regions are linked, suggesting that the PAS domain serves as a ligand-regulated switch for this eukaryotic signaling system.

Selected figure(s)

Figure 1.
Figure 1. Structural Features of PAS Domains

Figure 5.
Figure 5. Identification of the Kinase Binding Site on the Surface of hPASK PAS A

The above figures are reprinted by permission from Cell Press: Structure (2002, 10, 1349-1361) copyright 2002.

Figures were selected by the author.