1eu8
From Proteopedia
(New page: 200px<br /><applet load="1eu8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eu8, resolution 1.9Å" /> '''STRUCTURE OF TREHALOS...) |
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| - | [[Image:1eu8.gif|left|200px]]<br /><applet load="1eu8" size=" | + | [[Image:1eu8.gif|left|200px]]<br /><applet load="1eu8" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1eu8, resolution 1.9Å" /> | caption="1eu8, resolution 1.9Å" /> | ||
'''STRUCTURE OF TREHALOSE MALTOSE BINDING PROTEIN FROM THERMOCOCCUS LITORALIS'''<br /> | '''STRUCTURE OF TREHALOSE MALTOSE BINDING PROTEIN FROM THERMOCOCCUS LITORALIS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We report the crystallization and structure determination at 1.85 A of the | + | We report the crystallization and structure determination at 1.85 A 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 antiparallel 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1EU8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermococcus_litoralis Thermococcus litoralis] with PT, CL and TRE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1EU8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermococcus_litoralis Thermococcus litoralis] with <scene name='pdbligand=PT:'>PT</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=TRE:'>TRE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EU8 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: trehalose-maltose binding protein]] | [[Category: trehalose-maltose binding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:31:47 2008'' |
Revision as of 10:31, 21 February 2008
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STRUCTURE OF TREHALOSE MALTOSE BINDING PROTEIN FROM THERMOCOCCUS LITORALIS
Overview
We report the crystallization and structure determination at 1.85 A 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 antiparallel 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.
About this Structure
1EU8 is a Single protein structure of sequence from Thermococcus litoralis with , and as ligands. Full crystallographic information is available from OCA.
Reference
The crystal structure of a liganded trehalose/maltose-binding protein from the hyperthermophilic Archaeon Thermococcus litoralis at 1.85 A., Diez J, Diederichs K, Greller G, Horlacher R, Boos W, Welte W, J Mol Biol. 2001 Jan 26;305(4):905-15. PMID:11162101
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