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| | <StructureSection load='1ik6' size='340' side='right'caption='[[1ik6]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='1ik6' size='340' side='right'caption='[[1ik6]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ik6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_51768 Atcc 51768]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IK6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IK6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ik6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IK6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IK6 FirstGlance]. <br> |
| - | </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=1ik6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ik6 OCA], [http://pdbe.org/1ik6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ik6 RCSB], [http://www.ebi.ac.uk/pdbsum/1ik6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ik6 ProSAT]</span></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]] 2Å</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=1ik6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ik6 OCA], [https://pdbe.org/1ik6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ik6 RCSB], [https://www.ebi.ac.uk/pdbsum/1ik6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ik6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8ZUR7_PYRAE Q8ZUR7_PYRAE] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Pyruvate dehydrogenase|Pyruvate dehydrogenase]] | + | *[[Pyruvate dehydrogenase 3D structures|Pyruvate dehydrogenase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 51768]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Eisenberg, D]] | + | [[Category: Pyrobaculum aerophilum]] |
| - | [[Category: Kleiger, G]] | + | [[Category: Eisenberg D]] |
| - | [[Category: Perry, J]] | + | [[Category: Kleiger G]] |
| - | [[Category: E1beta]] | + | [[Category: Perry J]] |
| - | [[Category: Gxxxg]]
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| - | [[Category: Oxidoreductase]]
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| - | [[Category: Pyruvate dehydrogenase]]
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| - | [[Category: Tetramer]]
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| Structural highlights
Function
Q8ZUR7_PYRAE
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
As part of a structural genomics project, we have determined the 2.0 A structure of the E1beta subunit of pyruvate dehydrogenase from Pyrobaculum aerophilum (PA), a thermophilic archaeon. The overall fold of E1beta from PA is closely similar to the previously determined E1beta structures from humans (HU) and P. putida (PP). However, unlike the HU and PP structures, the PA structure was determined in the absence of its partner subunit, E1alpha. Significant structural rearrangements occur in E1beta when its E1alpha partner is absent, including rearrangement of several secondary structure elements such as helix C. Helix C is buried by E1alpha in the HU and PP structures, but makes crystal contacts in the PA structure that lead to an apparent beta(4) tetramer. Static light scattering and sedimentation velocity data are consistent with the formation of PA E1beta tetramers in solution. The interaction of helix C with its symmetry-related counterpart stabilizes the tetrameric interface, where two glycine residues on the same face of one helix create a packing surface for the other helix. This GPhiXXG helix-helix interaction motif has previously been found in interacting transmembrane helices, and is found here at the E1alpha-E1beta interface for both the HU and PP alpha(2)beta(2) tetramers. As a case study in structural genomics, this work illustrates that comparative analysis of protein structures can identify the structural significance of a sequence motif.
3D structure and significance of the GPhiXXG helix packing motif in tetramers of the E1beta subunit of pyruvate dehydrogenase from the archeon Pyrobaculum aerophilum.,Kleiger G, Perry J, Eisenberg D Biochemistry. 2001 Dec 4;40(48):14484-92. PMID:11724561[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kleiger G, Perry J, Eisenberg D. 3D structure and significance of the GPhiXXG helix packing motif in tetramers of the E1beta subunit of pyruvate dehydrogenase from the archeon Pyrobaculum aerophilum. Biochemistry. 2001 Dec 4;40(48):14484-92. PMID:11724561
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