PDBsum entry 4dg0

Transferase/transferase inhibitor

PDB id

4dg0

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Contents

			Protein chains

					341 a.a.


					20 a.a.

			Ligands

					MYR


					ANP

			Metals

					_MG ×2

			Waters ×344

PDB id:

4dg0

Links

Name:

Transferase/transferase inhibitor

Title:

Crystal structure of myristoylated wt catalytic subunit of camp- dependent protein kinase in complex with sp20 and amp-pnp

Structure:

Camp-dependent protein kinase catalytic subunit alpha. Chain: e. Fragment: unp residues 2-351. Synonym: pka c-alpha. Engineered: yes. Camp-dependent protein kinase inhibitor alpha. Chain: i. Fragment: unp residues 6-25. Synonym: pki-alpha, camp-dependent protein kinase inhibitor,

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Gene: prkaca, pkaca. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 10090

Resolution:

2.00Å

R-factor:

0.196

R-free:

0.228

Authors:

A.C.Bastidas,J.M.Steichen,S.S.Taylor

Key ref:

A.C.Bastidas et al. (2012). Role of N-terminal myristylation in the structure and regulation of cAMP-dependent protein kinase. J Mol Biol, 422, 215-229. PubMed id: 22617327

Date:

24-Jan-12

Release date:

06-Jun-12

PROCHECK

	Headers

	References

Protein chain

P05132 (KAPCA_MOUSE) - cAMP-dependent protein kinase catalytic subunit alpha from Mus musculus

Seq: Struc:					351 a.a. 341 a.a.*

Protein chain

P63248 (IPKA_MOUSE) - cAMP-dependent protein kinase inhibitor alpha from Mus musculus

Seq: Struc:					76 a.a. 20 a.a.*

Key:

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 3 residue positions (black crosses)



		Enzyme reactions

Enzyme class:

Chain E: E.C.2.7.11.11 - cAMP-dependent protein kinase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

1.	L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H⁺
2.	L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H⁺

L-seryl-[protein]	+	ATP	=	O-phospho-L-seryl-[protein] Bound ligand (Het Group name = ANP) matches with 81.25% similarity	+	ADP	+	H(+)

L-threonyl-[protein]	+	ATP	=	O-phospho-L-threonyl-[protein] Bound ligand (Het Group name = ANP) matches with 81.25% similarity	+	ADP	+	H(+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

	J Mol Biol 422:215-229 (2012)
PubMed id: 22617327

Role of N-terminal myristylation in the structure and regulation of cAMP-dependent protein kinase.
A.C.Bastidas, M.S.Deal, J.M.Steichen, M.M.Keshwani, Y.Guo, S.S.Taylor.

ABSTRACT

No abstract given.

Literature references that cite this PDB file's key reference

PubMed id

Reference

22992589

S.S.Taylor, R.Ilouz, P.Zhang, and A.P.Kornev (2012).
Assembly of allosteric macromolecular switches: lessons from PKA.

Nat Rev Mol Cell Biol, 13, 646-658.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.