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| | <StructureSection load='4rf6' size='340' side='right'caption='[[4rf6]], [[Resolution|resolution]] 1.95Å' scene=''> | | <StructureSection load='4rf6' size='340' side='right'caption='[[4rf6]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4rf6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Antja Antja]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RF6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RF6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4rf6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Anthopleura_japonica Anthopleura japonica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RF6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RF6 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4rf7|4rf7]], [[4rf8|4rf8]], [[4rf9|4rf9]]</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]] 1.95Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arginine_kinase Arginine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.3 2.7.3.3] </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=4rf6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rf6 OCA], [https://pdbe.org/4rf6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rf6 RCSB], [https://www.ebi.ac.uk/pdbsum/4rf6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rf6 ProSAT]</span></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=4rf6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rf6 OCA], [http://pdbe.org/4rf6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rf6 RCSB], [http://www.ebi.ac.uk/pdbsum/4rf6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rf6 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/KARG_ANTJA KARG_ANTJA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Antja]] | + | [[Category: Anthopleura japonica]] |
| - | [[Category: Arginine kinase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Qiao, Z]] | + | [[Category: Qiao Z]] |
| - | [[Category: Wang, Z]] | + | [[Category: Wang Z]] |
| - | [[Category: Ye, S]] | + | [[Category: Ye S]] |
| - | [[Category: Zhang, R]] | + | [[Category: Zhang R]] |
| - | [[Category: Double domain]]
| + | |
| - | [[Category: Phosphagen kinase]]
| + | |
| - | [[Category: Tandem domain]]
| + | |
| - | [[Category: Transferase]]
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| Structural highlights
Function
KARG_ANTJA
Publication Abstract from PubMed
Tandem duplications and fusions of single genes have led to magnificent expansions in the divergence of protein structures and functions over evolutionary timescales. One of the possible results is polydomain enzymes with interdomain cooperativities, few examples of which have been structurally characterized at the full-length level to explore their innate synergistic mechanisms. This work reports the crystal structures of a double-domain phosphagen kinase in both apo and ligand-bound states, revealing a novel asymmetric L-shaped arrangement of the two domains. Unexpectedly, the interdomain connections are not based on a flexible hinge linker but on a rigid secondary-structure element: a long alpha-helix that tethers the tandem domains in relatively fixed positions. Besides the connective helix, the two domains also contact each other directly and form an interdomain interface in which hydrogen bonds and hydrophobic interactions further stabilize the L-shaped domain arrangement. Molecular-dynamics simulations show that the interface is generally stable, suggesting that the asymmetric domain arrangement crystallographically observed in the present study is not a conformational state simply restrained by crystal-packing forces. It is possible that the asymmetrically arranged tandem domains could provide a structural basis for further studies of the interdomain synergy.
Structure of a double-domain phosphagen kinase reveals an asymmetric arrangement of the tandem domains.,Wang Z, Qiao Z, Ye S, Zhang R Acta Crystallogr D Biol Crystallogr. 2015 Apr;71(Pt 4):779-89. doi:, 10.1107/S1399004715001169. Epub 2015 Mar 26. PMID:25849389[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wang Z, Qiao Z, Ye S, Zhang R. Structure of a double-domain phosphagen kinase reveals an asymmetric arrangement of the tandem domains. Acta Crystallogr D Biol Crystallogr. 2015 Apr;71(Pt 4):779-89. doi:, 10.1107/S1399004715001169. Epub 2015 Mar 26. PMID:25849389 doi:http://dx.doi.org/10.1107/S1399004715001169
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