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| | <StructureSection load='3cwo' size='340' side='right'caption='[[3cwo]], [[Resolution|resolution]] 3.10Å' scene=''> | | <StructureSection load='3cwo' size='340' side='right'caption='[[3cwo]], [[Resolution|resolution]] 3.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3cwo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CWO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CWO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3cwo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CWO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CWO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 3.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1thf|1thf]], [[1tmy|1tmy]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3cwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cwo OCA], [http://pdbe.org/3cwo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cwo RCSB], [http://www.ebi.ac.uk/pdbsum/3cwo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3cwo 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=3cwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cwo OCA], [https://pdbe.org/3cwo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cwo RCSB], [https://www.ebi.ac.uk/pdbsum/3cwo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cwo ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/HIS6_THEMA HIS6_THEMA] IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.[HAMAP-Rule:MF_01013] |
| | == 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: Atcc 43589]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bharat, T A.M]] | + | [[Category: Thermotoga maritima]] |
| - | [[Category: Eisenbeis, S]] | + | [[Category: Bharat TAM]] |
| - | [[Category: Hocker, B]] | + | [[Category: Eisenbeis S]] |
| - | [[Category: Zeth, K]] | + | [[Category: Hocker B]] |
| - | [[Category: Chey]]
| + | [[Category: Zeth K]] |
| - | [[Category: De novo protein]]
| + | |
| - | [[Category: Half barrel]]
| + | |
| - | [[Category: Hisf]]
| + | |
| - | [[Category: Xray]]
| + | |
| Structural highlights
Function
HIS6_THEMA IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.[HAMAP-Rule:MF_01013]
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
Combinatorial assembly of protein domains plays an important role in the evolution of proteins. There is also evidence that protein domains have come together from stable subdomains. This concept of modular assembly could be used to construct new well folded proteins from stable protein fragments. Here, we report the construction of a chimeric protein from parts of a (betaalpha)(8)-barrel enzyme from histidine biosynthesis pathway (HisF) and a protein of the (betaalpha)(5)-flavodoxin-like fold (CheY) from Thermotoga maritima that share a high structural similarity. We expected this construct to fold into a full (betaalpha)(8)-barrel. Our results show that the chimeric protein is a stable monomer that unfolds with high cooperativity. Its three-dimensional structure, which was solved to 3.1 A resolution by x-ray crystallography, confirms a barrel-like fold in which the overall structures of the parent proteins are highly conserved. The structure further reveals a ninth strand in the barrel, which is formed by residues from the HisF C terminus and an attached tag. This strand invades between beta-strand 1 and 2 of the CheY part closing a gap in the structure that might be due to a suboptimal fit between the fragments. Thus, by a combination of parts from two different folds and a small arbitrary fragment, we created a well folded and stable protein.
A beta alpha-barrel built by the combination of fragments from different folds.,Bharat TA, Eisenbeis S, Zeth K, Hocker B Proc Natl Acad Sci U S A. 2008 Jul 22;105(29):9942-7. Epub 2008 Jul 15. PMID:18632584[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bharat TA, Eisenbeis S, Zeth K, Hocker B. A beta alpha-barrel built by the combination of fragments from different folds. Proc Natl Acad Sci U S A. 2008 Jul 22;105(29):9942-7. Epub 2008 Jul 15. PMID:18632584
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