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6czm
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Medicago truncatula ATP-phosphoribosyltransferase in tense form== | |
| + | <StructureSection load='6czm' size='340' side='right' caption='[[6czm]], [[Resolution|resolution]] 2.88Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6czm]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CZM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CZM FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=HIS:HISTIDINE'>HIS</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=6czm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6czm OCA], [http://pdbe.org/6czm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6czm RCSB], [http://www.ebi.ac.uk/pdbsum/6czm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6czm ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In the first committed step of histidine biosynthesis, ATP and 5-phosphoribosyl-alpha1-pyrophosphate (PRPP), in a presence of ATP phosphoribosyltransferase (ATP-PRT, EC 2.4.2.17), yield phosphoribosyl-ATP. ATP-PRTs are subject to feedback inhibition by histidine, that allosterically binds between the regulatory domains. Histidine biosynthetic pathways of bacteria, lower eukaryotes, and plants are considered promising targets for a design of antibiotics, antifungal agents, and herbicides because higher organisms are histidine heterotrophs. Plant ATP-PRTs are similar to one of the two types of their bacterial counterparts, the long-type ATP-PRTs. A biochemical and structural study of ATP-PRT from the model legume plant, Medicago truncatula ( Medtr ATP-PRT1) is reported herein. Two crystal structures, presenting homohexameric Medtr ATP-PRT1 in its relaxed (R-) and histidine-bound, tense (T-) states allowed to observe key features of the enzyme and provided the first structural insights into an ATP-PRT from a eukaryotic organism. In particular, they show pronounced conformational reorganizations during R-state to T-state transition that involves substantial movements of domains. This rearrangement requires a trans - to cis - switch of a peptide backbone within the hinge region of Medtr ATP-PRT1. A C-terminal alpha-helix, absent in bacteria, reinforces the hinge that is constituted by two peptide strands. As a result, conformations of the R- and T-states are significantly different from the corresponding states of prokaryotic enzymes with known 3-D structures. Lastly, AMP bound at the active site is consistent with a competitive (and synergistic with histidine) nature of AMP inhibition. | ||
| - | + | Guarding the gateway to histidine biosynthesis in plants: Medicago truncatula ATP-phosphoribosyltransferase in relaxed and tense states.,Ruszkowski M Biochem J. 2018 Aug 2. pii: BCJ20180289. doi: 10.1042/BCJ20180289. PMID:30072492<ref>PMID:30072492</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 6czm" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Ruszkowski, M]] | [[Category: Ruszkowski, M]] | ||
| + | [[Category: Allosteric regulation]] | ||
| + | [[Category: Atp-prt]] | ||
| + | [[Category: Histidine biosynthesis]] | ||
| + | [[Category: Prpp]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 16:15, 15 August 2018
Crystal structure of Medicago truncatula ATP-phosphoribosyltransferase in tense form
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