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| | ==Crystal Structure of E.coli transthyretin-related protein with bound Zn and Br== | | ==Crystal Structure of E.coli transthyretin-related protein with bound Zn and Br== |
| - | <StructureSection load='2g2p' size='340' side='right' caption='[[2g2p]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='2g2p' size='340' side='right'caption='[[2g2p]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2g2p]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G2P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2G2P FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2g2p]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G2P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G2P FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2g2n|2g2n]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2g2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g2p OCA], [http://pdbe.org/2g2p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2g2p RCSB], [http://www.ebi.ac.uk/pdbsum/2g2p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2g2p ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2g2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g2p OCA], [https://pdbe.org/2g2p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g2p RCSB], [https://www.ebi.ac.uk/pdbsum/2g2p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g2p ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HIUH_ECOLI HIUH_ECOLI]] Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU). | + | [https://www.uniprot.org/uniprot/HIUH_ECOLI HIUH_ECOLI] Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: Backstrom, S]] | + | [[Category: Large Structures]] |
| - | [[Category: Lundberg, E]] | + | [[Category: Backstrom S]] |
| - | [[Category: Sauer, U H]] | + | [[Category: Lundberg E]] |
| - | [[Category: Sauer-Eriksson, A E]] | + | [[Category: Sauer UH]] |
| - | [[Category: Transthyretin]] | + | [[Category: Sauer-Eriksson AE]] |
| - | [[Category: Transthyretin-related protein]]
| + | |
| - | [[Category: Unknown function]]
| + | |
| Structural highlights
Function
HIUH_ECOLI Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lundberg E, Backstrom S, Sauer UH, Sauer-Eriksson AE. The transthyretin-related protein: structural investigation of a novel protein family. J Struct Biol. 2006 Sep;155(3):445-57. Epub 2006 May 8. PMID:16723258 doi:10.1016/j.jsb.2006.04.002
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