2g2p
From Proteopedia
(New page: 200px<br /><applet load="2g2p" size="450" color="white" frame="true" align="right" spinBox="true" caption="2g2p, resolution 2.10Å" /> '''Crystal Structure of...) |
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| - | [[Image:2g2p.jpg|left|200px]]<br /><applet load="2g2p" size=" | + | [[Image:2g2p.jpg|left|200px]]<br /><applet load="2g2p" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2g2p, resolution 2.10Å" /> | caption="2g2p, resolution 2.10Å" /> | ||
'''Crystal Structure of E.coli transthyretin-related protein with bound Zn and Br'''<br /> | '''Crystal Structure of E.coli transthyretin-related protein with bound Zn and Br'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The transthyretin-related protein (TRP) family comprises proteins | + | The transthyretin-related protein (TRP) family comprises proteins predicted to be structurally related to the homotetrameric transport protein transthyretin (TTR). The function of TRPs is not yet fully established, but recent data suggest that they are involved in purine catabolism. We have determined the three-dimensional structure of the Escherichia coli TRP in two crystal forms; one at 1.65 A resolution in the presence of zinc, and the other at 2.1 A resolution in the presence of zinc and bromide. The structures revealed five zinc-ion-binding sites per monomer. Of these, the zinc ions bound at sites I and II are coordinated in tetrahedral geometries to the side chains of residues His9, His96, His98, Ser114, and three water molecules at the putative ligand-binding site. Of these four residues, His9, His98, and Ser114 are conserved. His9 and His98 bind the central zinc (site I) together with two water molecules. The side chain of His98 also binds to the zinc ion at site II. Bromide ions bind at site I only, replacing one of the water molecules coordinated to the zinc ion. The C-terminal four amino acid sequence motif Y-[RK]-G-[ST] constitutes the signature sequence of the TRP family. Two Tyr111 residues form direct hydrogen bonds to each other over the tetramer interface at the area, which in TTR constitutes the rear part of its thyroxine-binding channel. The putative substrate/ligand-binding channel of TRP is consequently shallower and broader than its counterpart in TTR. |
==About this Structure== | ==About this Structure== | ||
| - | 2G2P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN, BR and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2G2P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=BR:'>BR</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G2P OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Backstrom, S.]] | [[Category: Backstrom, S.]] | ||
[[Category: Lundberg, E.]] | [[Category: Lundberg, E.]] | ||
| - | [[Category: Sauer, U | + | [[Category: Sauer, U H.]] |
| - | [[Category: Sauer-Eriksson, A | + | [[Category: Sauer-Eriksson, A E.]] |
[[Category: BR]] | [[Category: BR]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: transthyretin-related protein]] | [[Category: transthyretin-related protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:27:34 2008'' |
Revision as of 15:27, 21 February 2008
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Crystal Structure of E.coli transthyretin-related protein with bound Zn and Br
Overview
The transthyretin-related protein (TRP) family comprises proteins predicted to be structurally related to the homotetrameric transport protein transthyretin (TTR). The function of TRPs is not yet fully established, but recent data suggest that they are involved in purine catabolism. We have determined the three-dimensional structure of the Escherichia coli TRP in two crystal forms; one at 1.65 A resolution in the presence of zinc, and the other at 2.1 A resolution in the presence of zinc and bromide. The structures revealed five zinc-ion-binding sites per monomer. Of these, the zinc ions bound at sites I and II are coordinated in tetrahedral geometries to the side chains of residues His9, His96, His98, Ser114, and three water molecules at the putative ligand-binding site. Of these four residues, His9, His98, and Ser114 are conserved. His9 and His98 bind the central zinc (site I) together with two water molecules. The side chain of His98 also binds to the zinc ion at site II. Bromide ions bind at site I only, replacing one of the water molecules coordinated to the zinc ion. The C-terminal four amino acid sequence motif Y-[RK]-G-[ST] constitutes the signature sequence of the TRP family. Two Tyr111 residues form direct hydrogen bonds to each other over the tetramer interface at the area, which in TTR constitutes the rear part of its thyroxine-binding channel. The putative substrate/ligand-binding channel of TRP is consequently shallower and broader than its counterpart in TTR.
About this Structure
2G2P is a Single protein structure of sequence from Escherichia coli with , and as ligands. Full crystallographic information is available from OCA.
Reference
The transthyretin-related protein: structural investigation of a novel protein family., Lundberg E, Backstrom S, Sauer UH, Sauer-Eriksson AE, J Struct Biol. 2006 Sep;155(3):445-57. Epub 2006 May 8. PMID:16723258
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