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4g78

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==Subatomic Resolution Crystal Structure of Histidine-containing Phosphotransfer Protein MtHPt2 from Medicago truncatula==
==Subatomic Resolution Crystal Structure of Histidine-containing Phosphotransfer Protein MtHPt2 from Medicago truncatula==
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<StructureSection load='4g78' size='340' side='right' caption='[[4g78]], [[Resolution|resolution]] 0.92&Aring;' scene=''>
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<StructureSection load='4g78' size='340' side='right'caption='[[4g78]], [[Resolution|resolution]] 0.92&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4g78]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Barrel_medic Barrel medic]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G78 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G78 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4g78]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Medicago_truncatula Medicago truncatula]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G78 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G78 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3us6|3us6]], [[1yvi|1yvi]], [[2q4f|2q4f]], [[1wn0|1wn0]], [[1qsp|1qsp]]</td></tr>
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</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=4g78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g78 OCA], [https://pdbe.org/4g78 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g78 RCSB], [https://www.ebi.ac.uk/pdbsum/4g78 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g78 ProSAT]</span></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MtHPt2, MTR_1g089130, MTR_1g089350 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3880 Barrel medic])</td></tr>
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<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=4g78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g78 OCA], [http://pdbe.org/4g78 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4g78 RCSB], [http://www.ebi.ac.uk/pdbsum/4g78 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4g78 ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/G7I2T8_MEDTR G7I2T8_MEDTR]
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Arabidopsis thaliana histidine phosphotransfer proteins (AHPs) are similar to bacterial and yeast histidine phosphotransfer proteins (HPts), which act in multistep phosphorelay signaling pathways. A phosphorelay pathway is the current model for cytokinin signaling. To assess the role of AHPs in cytokinin signaling, we isolated T-DNA insertions in the five AHP genes that are predicted to encode functional HPts and constructed multiple insertion mutants, including an ahp1,2,3,4,5 quintuple mutant. Single ahp mutants were indistinguishable from wild-type seedlings in cytokinin response assays. However, various higher-order mutants displayed reduced sensitivity to cytokinin in diverse cytokinin assays, indicating both a positive role for AHPs in cytokinin signaling and functional overlap among the AHPs. In contrast with the other four AHPs, AHP4 may play a negative role in some cytokinin responses. The quintuple ahp mutant showed various abnormalities in growth and development, including reduced fertility, increased seed size, reduced vascular development, and a shortened primary root. These data indicate that most of the AHPs are redundant, positive regulators of cytokinin signaling and affect multiple aspects of plant development.
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The Arabidopsis histidine phosphotransfer proteins are redundant positive regulators of cytokinin signaling.,Hutchison CE, Li J, Argueso C, Gonzalez M, Lee E, Lewis MW, Maxwell BB, Perdue TD, Schaller GE, Alonso JM, Ecker JR, Kieber JJ Plant Cell. 2006 Nov;18(11):3073-87. Epub 2006 Nov 22. PMID:17122069<ref>PMID:17122069</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4g78" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Barrel medic]]
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[[Category: Large Structures]]
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[[Category: Jaskolski, M]]
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[[Category: Medicago truncatula]]
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[[Category: Ruszkowski, M]]
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[[Category: Jaskolski M]]
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[[Category: Sikorski, M]]
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[[Category: Ruszkowski M]]
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[[Category: Helix bundle]]
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[[Category: Sikorski M]]
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[[Category: Histidine kinase]]
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[[Category: Plant hormone signal transduction]]
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[[Category: Subatomic resolution]]
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[[Category: Transferase]]
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Revision as of 20:28, 19 October 2022

Subatomic Resolution Crystal Structure of Histidine-containing Phosphotransfer Protein MtHPt2 from Medicago truncatula

PDB ID 4g78

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