PDBsum entry 2pc6

Lyase

PDB id: 2pc6

Contents

Protein chains

164 a.a. *

Ligands

UNL ×3

Metals

_CA ×3

Waters ×200

* Residue conservation analysis

PDB id:

2pc6

Name:

Lyase

Title:

Crystal structure of putative acetolactate synthase- small subunit from nitrosomonas europaea

Structure:

Probable acetolactate synthase isozyme iii (small subunit). Chain: a, b, c, d. Engineered: yes

Source:

Nitrosomonas europaea atcc 19718. Organism_taxid: 228410. Strain: ifo 14298. Gene: ilvh, ne1324. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.50Å R-factor: 0.208 R-free: 0.276

Authors:

J.J.Petkowski,M.Chruszcz,M.D.Zimmerman,H.Zheng,M.T.Cymborowski, T.Skarina,O.Onopriyenko,A.Savchenko,A.Edwards,W.Minor,A.Joachimiak, Midwest Center For Structural Genomics (Mcsg)

Key ref:

J.J.Petkowski et al. (2007). Crystal structures of TM0549 and NE1324--two orthologs of E. coli AHAS isozyme III small regulatory subunit. Protein Sci, 16, 1360-1367. PubMed id: 17586771 DOI: 10.1110/ps.072793807

Date:

29-Mar-07 Release date: 10-Apr-07

Supersedes:

2fgd

Protein chains

Q82UZ2  (Q82UZ2_NITEU) -  Acetolactate synthase small subunit from Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298)

Seq: 163 a.a.

Struc: 164 a.a.

Enzyme reactions

• Enzyme class: E.C.2.2.1.6 - acetolactate synthase.
• Pathway: Isoleucine and Valine Biosynthesis
• Reaction: 2 pyruvate + H⁺ = (2S)-2-acetolactate + CO2

2 × pyruvate + H(+) (Bound ligand (Het Group name = UNL) matches with 70.00% similarity) = (2S)-2-acetolactate + CO2

• Cofactor: Thiamine diphosphate

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

reference

DOI no: 10.1110/ps.072793807

Protein Sci 16:1360-1367 (2007)

PubMed id: 17586771

Crystal structures of TM0549 and NE1324--two orthologs of E. coli AHAS isozyme III small regulatory subunit.

J.J.Petkowski, M.Chruszcz, M.D.Zimmerman, H.Zheng, T.Skarina, O.Onopriyenko, M.T.Cymborowski, K.D.Koclega, A.Savchenko, A.Edwards, W.Minor.

ABSTRACT

Crystal structures of two orthologs of the regulatory subunit of acetohydroxyacid synthase III (AHAS, EC 2.2.1.6) from Thermotoga maritima (TM0549) and Nitrosomonas europea (NE1324) were determined by single-wavelength anomalous diffraction methods with the use of selenomethionine derivatives at 2.3 A and 2.5 A, respectively. TM0549 and NE1324 share the same fold, and in both proteins the polypeptide chain contains two separate domains of a similar size. Each protein contains a C-terminal domain with ferredoxin-type fold and an N-terminal ACT domain, of which the latter is characteristic for several proteins involved in amino acid metabolism. The ferredoxin domain is stabilized by a calcium ion in the crystal structure of NE1324 and by a Mg(H2O)(6)2+ ion in TM0549. Both TM0549 and NE1324 form dimeric assemblies in the crystal lattice.

Selected figure(s)

Figure 2.
Figure 2. (A) Sequence alignment of NE1324 (NE), SSU from E. coli (EC), and TM0549 (TM). Conserved amino acids marked by

The above figure is reprinted by permission from the Protein Society: Protein Sci (2007, 16, 1360-1367) copyright 2007.

Figure was selected by an automated process.