+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

The crystal structure of a liganded trehalose/maltose-binding protein from the hyperthermophilic Archaeon Thermococcus litoralis at 1.85 A



The crystal structure of a liganded trehalose/maltose-binding protein from the hyperthermophilic Archaeon Thermococcus litoralis at 1.85 A



Journal of Molecular Biology 305(4): 905-915



We report the crystallization and structure determination at 1.85 ANG of the extracellular, membrane-anchored trehalose/maltose-binding protein (TMBP) in complex with its substrate trehalose. TMBP is the substrate recognition site of the high-affinity trehalose/maltose ABC transporter of the hyperthermophilic Archaeon Thermococcus litoralis. In vivo, this protein is anchored to the membrane, presumably via an N-terminal cysteine lipid modification. The crystallized protein was N-terminally truncated, resulting in a soluble protein exhibiting the same binding characteristics as the wild-type protein. The protein shows the characteristic features of a transport-related, substrate-binding protein and is structurally related to the maltose-binding protein (MBP) of Escherichia coli. It consists of two similar lobes, each formed by a parallel beta-sheet flanked by alpha-helices on both sides. Both are connected by a hinge region consisting of two anti-parallel beta-strands and an alpha-helix. As in MBP, the substrate is bound in the cleft between the lobes by hydrogen bonds and hydrophobic interactions. However, compared to maltose binding in MBP, direct hydrogen bonding between the substrate and the protein prevails while apolar contacts are reduced. To elucidate factors contributing to thermostability, we compared TMBP with its mesophilic counterpart MBP and found differences known from similar investigations. Specifically, we find helices that are longer than their structurally equivalent counterparts, and fewer internal cavities.

Please choose payment method:






(PDF emailed within 0-6 h: $19.90)

Accession: 047603096

Download citation: RISBibTeXText

PMID: 11162101

DOI: 10.1006/jmbi.2000.4203


Related references

D-trehalose/D-maltose-binding protein from the hyperthermophilic archaeon Thermococcus litoralis: the binding of trehalose and maltose results in different protein conformational states. Proteins 63(4): 754-767, 2006

Temperature modulates binding specificity and affinity of the d-trehalose/d-maltose-binding protein from the hyperthermophilic archaeon Thermococcus litoralis. Biochimica et Biophysica Acta 1774(5): 540-544, 2007

Molecular adaptation strategies to high temperature and thermal denaturation mechanism of the D-trehalose/D-maltose-binding protein from the hyperthermophilic archaeon Thermococcus litoralis. Proteins 67(4): 1002-1009, 2007

Archaeal binding protein-dependent ABC transporter: molecular and biochemical analysis of the trehalose/maltose transport system of the hyperthermophilic archaeon Thermococcus litoralis. Journal of Bacteriology 180(3): 680-689, 1998

Enzymes and proteins from extremophiles as hyperstable probes in nanotechnology: the use of D-trehalose/D-maltose-binding protein from the hyperthermophilic archaeon Thermococcus litoralis for sugars monitoring. Extremophiles 12(1): 69-73, 2008

Pressure effects on the structure and stability of the hyperthermophilic trehalose/maltose-binding protein from Thermococcus litoralis. Journal of Physical Chemistry. B 113(38): 12804-8, 2009

Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis. Embo Journal 19(22): 5951-5961, 2000

High-affinity maltose/trehalose transport system in the hyperthermophilic archaeon Thermococcus litoralis. Journal of Bacteriology 178(16): 4773-4777, 1996

Purification and characterization of the heterologously expressed trehalose/maltose ABC transporter complex of the hyperthermophilic archaeon Thermococcus litoralis. European Journal of Biochemistry 268(14): 4011-4018, 2001

TrmB, a sugar-specific transcriptional regulator of the trehalose/maltose ABC transporter from the hyperthermophilic archaeon Thermococcus litoralis. Journal of Biological Chemistry 278(2): 983-990, 2003

Molecular and biochemical analysis of MalK, the ATP-hydrolyzing subunit of the trehalose/maltose transport system of the hyperthermophilic archaeon Thermococcus litoralis. Journal of Biological Chemistry 274(29): 20259-20264, 1999

Maltose metabolism in the hyperthermophilic archaeon Thermococcus litoralis. Abstracts of the General Meeting of the American Society for Microbiology 100: 433, 2000

TreT, a novel trehalose glycosyltransferring synthase of the hyperthermophilic archaeon Thermococcus litoralis. Journal of Biological Chemistry 279(46): 47890-7, 2004

Maltose metabolism in the hyperthermophilic archaeon Thermococcus litoralis: purification and characterization of key enzymes. Journal of Bacteriology 181(11): 3358-3367, 1999

Stability of sugar-binding proteins: D-galactose/D-glucose-binding protein from Escherichia coli and trehalose/maltose-binding protein from Thermococcus litoralis. Tsitologiia 52(11): 950-954, 2010