PDBsum entry 1r0c

Transferase

PDB id

1r0c

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Contents

			Protein chains

					310 a.a. *


					153 a.a. *

			Ligands

					PO4 ×2


					NCD ×2

			Metals

					_ZN ×2

			Waters ×553

* Residue conservation analysis

PDB id:

1r0c

Links

Name:

Transferase

Title:

Products in the t state of aspartate transcarbamylase: crystal structure of the phosphate and n-carbamyl-l-aspartate ligated enzyme

Structure:

Aspartate carbamoyltransferase catalytic chain. Chain: a, g. Synonym: aspartate transcarbamylase, atcase. Engineered: yes. Aspartate carbamoyltransferase regulatory chain. Chain: b, h. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Gene: pyrb or b4245 or c5345 or z5856 or ecs5222 or sf4245 or s4507. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: pyri or b4244 or c5344 or z5855 or ecs5221.

Biol. unit:

Dodecamer (from PDB file)

Resolution:

2.37Å

R-factor:

0.226

R-free:

0.274

Authors:

J.Huang,W.N.Lipscomb

Key ref:

J.Huang and W.N.Lipscomb (2004). Products in the T-state of aspartate transcarbamylase: crystal structure of the phosphate and N-carbamyl-L-aspartate ligated enzyme. Biochemistry, 43, 6422-6426. PubMed id: 15157076 DOI: 10.1021/bi0302144

Date:

19-Sep-03

Release date:

08-Jun-04

PROCHECK

	Headers

	References

Protein chains

P0A786 (PYRB_ECOLI) - Aspartate carbamoyltransferase catalytic subunit from Escherichia coli (strain K12)

Seq: Struc:					311 a.a. 310 a.a.

Protein chains

P0A7F3 (PYRI_ECOLI) - Aspartate carbamoyltransferase regulatory chain from Escherichia coli (strain K12)

Seq: Struc:					153 a.a. 153 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

Chains A, G: E.C.2.1.3.2 - aspartate carbamoyltransferase.

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

Pathway:

Pyrimidine Biosynthesis

Reaction:

carbamoyl phosphate + L-aspartate = N-carbamoyl-L-aspartate + phosphate + H⁺

carbamoyl phosphate

L-aspartate

N-carbamoyl-L-aspartate

phosphate
Bound ligand (Het Group name = NCD)
corresponds exactly

H(+)
Bound ligand (Het Group name = PO4)
corresponds exactly

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

reference

DOI no: 10.1021/bi0302144	Biochemistry 43:6422-6426 (2004)
PubMed id: 15157076

Products in the T-state of aspartate transcarbamylase: crystal structure of the phosphate and N-carbamyl-L-aspartate ligated enzyme.
J.Huang, W.N.Lipscomb.

ABSTRACT

The structure of aspartate transcarbamylase of Escherichia coli ligated to products (phosphate and N-carbamyl-l-aspartate) has been determined at 2.37 A resolution (R-factor = 0.23, R(free) = 0.27). Results might indicate a product release mode, rather than close analogues to the transition state like those found in our earlier studies of other ligands (N-phosphonacetyl-L-aspartate, carbamyl phosphate plus malonate, phosphonoacetamide plus malonate, or citrate plus phosphate). Ordered product release, first carbamylaspartate (CLA) and then phosphate, might be facilitated by a 4 A movement of phosphate from the substrate-analogue position to the product (phosphate) binding position, and by a somewhat similar release movement of the other product (CLA) relative to its analogue (citrate). This movement is consistent with earlier studies of binding of either pyrophosphate or phosphate alone [Honzatko, R. B., and Lipscomb, W. N. (1982) J. Mol. Biol. 160, 265-286].

Literature references that cite this PDB file's key reference

PubMed id

Reference

18618694

K.A.Stieglitz, J.Xia, and E.R.Kantrowitz (2009).
The first high pH structure of Escherichia coli aspartate transcarbamoylase.

Proteins, 74, 318-327.

PDB code:

3d7s

16741992

D.Shi, X.Yu, L.Roth, H.Morizono, M.Tuchman, and N.M.Allewell (2006).
Structures of N-acetylornithine transcarbamoylase from Xanthomonas campestris complexed with substrates and substrate analogs imply mechanisms for substrate binding and catalysis.

Proteins, 64, 532-542.

PDB codes:

1zq2 1zq6 1zq8 3kzm 3kzn 3kzo

16511017

D.De Vos, P.Hulpiau, B.Vergauwen, S.N.Savvides, and J.Van Beeumen (2005).
Expression, purification, crystallization and preliminary X-ray crystallographic studies of a cold-adapted aspartate carbamoyltransferase from Moritella profunda.

Acta Crystallogr Sect F Struct Biol Cryst Commun, 61, 279-281.

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. Where a reference describes a PDB structure, the PDB code is shown on the right.