PDBsum entry 3c9t

Transferase

PDB id

3c9t

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Contents

			Protein chains

					307 a.a. *

			Ligands

					TPS ×2


					ACP ×2

			Metals

					_MG ×10

			Waters ×14

* Residue conservation analysis

PDB id:

3c9t

Links

Name:

Transferase

Title:

Aathil complexed with amppcp and tmp

Structure:

Thiamine monophosphate kinase. Chain: a, b. Engineered: yes

Source:

Aquifex aeolicus. Organism_taxid: 63363. Gene: thil. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.60Å

R-factor:

0.213

R-free:

0.270

Authors:

K.M.Mcculloch,C.Kinsland,T.P.Begley,S.E.Ealick

Key ref:

K.M.McCulloch et al. (2008). Structural studies of thiamin monophosphate kinase in complex with substrates and products. Biochemistry, 47, 3810-3821. PubMed id: 18311927

Date:

18-Feb-08

Release date:

18-Mar-08

PROCHECK

	Headers

	References

Protein chains

O67883 (THIL_AQUAE) - Thiamine-monophosphate kinase from Aquifex aeolicus (strain VF5)

Seq: Struc:					306 a.a. 307 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.2.7.4.16 - thiamine-phosphate kinase.

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

Reaction:

thiamine phosphate + ATP = thiamine diphosphate + ADP

thiamine phosphate

ATP
Bound ligand (Het Group name = TPS)
corresponds exactly

thiamine diphosphate
Bound ligand (Het Group name = ACP)
matches with 81.25% similarity

ADP

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

reference

	Biochemistry 47:3810-3821 (2008)
PubMed id: 18311927

Structural studies of thiamin monophosphate kinase in complex with substrates and products.
K.M.McCulloch, C.Kinsland, T.P.Begley, S.E.Ealick.

ABSTRACT

Thiamin monophosphate kinase (ThiL) catalyzes the ATP-dependent phosphorylation of thiamin monophosphate (TMP) to form thiamin pyrophosphate (TPP), the active form of vitamin B 1. ThiL is a member of a small ATP binding superfamily that also includes the purine biosynthetic enzymes, PurM and PurL, NiFe hydrogenase maturation protein, HypE, and selenophosphate synthase, SelD. The latter four enzymes are believed to utilize phosphorylated intermediates during catalysis. To understand the mechanism of ThiL and its relationship to the other superfamily members, we determined the structure of Aquifex aeolicus ThiL (AaThiL) with nonhydrolyzable AMP-PCP and TMP, and also with the products of the reaction, ADP and TPP. The results suggest that AaThiL utilizes a direct, inline transfer of the gamma-phosphate of ATP to TMP rather than a phosphorylated enzyme intermediate. The structure of ThiL is compared to those of PurM, PurL, and HypE, and the ATP binding site is compared to that of PurL, for which nucleotide complexes are available.

Literature references that cite this PDB file's key reference

PubMed id

Reference

20633228

M.J.Gray, and J.C.Escalante-Semerena (2010).
A new pathway for the synthesis of α-ribazole-phosphate in Listeria innocua.

Mol Microbiol, 77, 1429-1438.

19923213

M.R.Challand, F.T.Martins, and P.L.Roach (2010).
Catalytic activity of the anaerobic tyrosine lyase required for thiamine biosynthesis in Escherichia coli.

J Biol Chem, 285, 5240-5248.

19348578

C.T.Jurgenson, T.P.Begley, and S.E.Ealick (2009).
The structural and biochemical foundations of thiamin biosynthesis.

Annu Rev Biochem, 78, 569-603.

18712276

Y.Zhang, M.Morar, and S.E.Ealick (2008).
Structural biology of the purine biosynthetic pathway.

Cell Mol Life Sci, 65, 3699-3724.

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.