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==Crystal Structure of adenosine phosphate-isopentenyltransferase complexed with diphosphate==
==Crystal Structure of adenosine phosphate-isopentenyltransferase complexed with diphosphate==
<StructureSection load='2ze8' size='340' side='right' caption='[[2ze8]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='2ze8' size='340' side='right'caption='[[2ze8]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2ze8]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"achromobacter_radiobacter"_(beijerinck_and_van_delden_1902)_bergey_et_al._1934 "achromobacter radiobacter" (beijerinck and van delden 1902) bergey et al. 1934]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZE8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZE8 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2ze8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZE8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZE8 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</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]] 2.8&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ze5|2ze5]], [[2ze6|2ze6]], [[2ze7|2ze7]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tzs ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=358 "Achromobacter radiobacter" (Beijerinck and van Delden 1902) Bergey et al. 1934])</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=2ze8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ze8 OCA], [https://pdbe.org/2ze8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ze8 RCSB], [https://www.ebi.ac.uk/pdbsum/2ze8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ze8 ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenylate_dimethylallyltransferase_(AMP-dependent) Adenylate dimethylallyltransferase (AMP-dependent)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.27 2.5.1.27] </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=2ze8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ze8 OCA], [http://pdbe.org/2ze8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ze8 RCSB], [http://www.ebi.ac.uk/pdbsum/2ze8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ze8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/IPTZ_AGRT5 IPTZ_AGRT5]] Transfers dimethylallyl groups to AMP as part of the biosynthesis of cytokinin phytohormones.  
[https://www.uniprot.org/uniprot/IPTZ_AGRFC IPTZ_AGRFC] Transfers dimethylallyl groups to AMP as part of the biosynthesis of cytokinin phytohormones.[REFERENCE:5]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ze8 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ze8 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The phytohormone cytokinin regulates plant growth and development. This hormone is also synthesized by some phytopathogenic bacteria, such as Agrobacterium tumefaciens, and is as a key factor in the formation of plant tumors. The rate-limiting step of cytokinin biosynthesis is catalyzed by adenosine phosphate-isopentenyltransferase (IPT). Agrobacterium IPT has a unique substrate specificity that enables it to increase trans-zeatin production by recruiting a metabolic intermediate of the host plant's biosynthetic pathway. Here, we show the crystal structures of Tzs, an IPT from A. tumefaciens, complexed with AMP and a prenyl-donor analogue, dimethylallyl S-thiodiphosphate. The structures reveal that the carbon-nitrogen-based prenylation proceeds by the SN2-reaction mechanism. Site-directed mutagenesis was used to determine the amino acid residues, Asp-173 and His-214, which are responsible for differences in prenyl-donor substrate specificity between plant and bacterial IPTs. IPT and the p loop-containing nucleoside triphosphate hydrolases likely evolved from a common ancestral protein. Despite structural similarities, IPT has evolved a distinct role in which the p loop transfers a prenyl moiety in cytokinin biosynthesis.
Structural insight into the reaction mechanism and evolution of cytokinin biosynthesis.,Sugawara H, Ueda N, Kojima M, Makita N, Yamaya T, Sakakibara H Proc Natl Acad Sci U S A. 2008 Feb 19;105(7):2734-9. Epub 2008 Feb 7. PMID:18258747<ref>PMID:18258747</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2ze8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Sakakibara, H]]
[[Category: Agrobacterium tumefaciens]]
[[Category: Crown gall tumor]]
[[Category: Large Structures]]
[[Category: Cytokinin biosynthesis]]
[[Category: Sakakibara H]]
[[Category: Transferase]]
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