The three-dimensional structure of diaminopimelate decarboxylase from Mycobacterium tuberculosis reveals a tetrameric enzyme organisation

The three-dimensional structure of the enzyme diaminopimelate decarboxylase from Mycobacterium tuberculosis has been determined in a new crystal form and refined to a resolution of 2.33 A. The monoclinic crystals contain one tetramer exhibiting D(2)-symmetry in the asymmetric unit. The tetramer exhibits a donut-like structure with a hollow interior. All four active sites are accessible only from the interior of the tetrameric assembly. Small-angle X-ray scattering indicates that in solution the predominant oligomeric species of the protein is a dimer, but also that higher oligomers exist at higher protein concentrations. The observed scattering data are best explained by assuming a dimer-tetramer equilibrium with about 7% tetramers present in solution. Consequently, at the elevated protein concentrations in the crowded environment inside the cell the observed tetramer may constitute the biologically relevant functional unit of the enzyme.

Medienart:

E-Artikel

Erscheinungsjahr:

2009

Erschienen:

2009

Enthalten in:

Zur Gesamtaufnahme - volume:10

Enthalten in:

Journal of structural and functional genomics - 10(2009), 3 vom: 21. Sept., Seite 209-17

Sprache:

Englisch

Beteiligte Personen:

Weyand, Simone [VerfasserIn]
Kefala, Georgia [VerfasserIn]
Svergun, Dmitri I [VerfasserIn]
Weiss, Manfred S [VerfasserIn]

Links:

Volltext

Themen:

Bacterial Proteins
Carboxy-Lyases
Comparative Study
Diaminopimelic acid decarboxylase
EC 4.1.1.-
EC 4.1.1.20
Journal Article
K3Z4F929H6
Lysine
Research Support, Non-U.S. Gov't

Anmerkungen:

Date Completed 11.01.2010

Date Revised 20.10.2021

published: Print-Electronic

Citation Status MEDLINE

doi:

10.1007/s10969-009-9065-z

funding:

Förderinstitution / Projekttitel:

PPN (Katalog-ID):

NLM189448903