7x98
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==5-Aminolevulinate synthase HemA from Rhodopseudomonas palustris== | |
| + | <StructureSection load='7x98' size='340' side='right'caption='[[7x98]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7x98]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodopseudomonas_palustris Rhodopseudomonas palustris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7X98 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7X98 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></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=7x98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7x98 OCA], [https://pdbe.org/7x98 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7x98 RCSB], [https://www.ebi.ac.uk/pdbsum/7x98 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7x98 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/M1FRN3_RHOPL M1FRN3_RHOPL] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 5-ALA is the precursor of all tetrapyrroles. 5-Aminolevulinate synthase (ALAS) catalyzes the production of 5-aminolevulinic acid (5-ALA) from glycine and succinyl-CoA. HemA from Rhodopseudomonas palustris (Rp-HemA) was reported to be a highly active ALAS. To understand the catalytic mechanism of Rp-HemA, the 2.05 A resolution crystal structure of Rp-HemA was solved. Open, half close and close conformations were observed in the substrate-free structures. Structure comparison and sequence alignment suggest the newly observed half close conformation may also be conserved in ALAS family. The pre-existed close and half close conformations in Rp-HemA may play a key role for its high activity. | ||
| - | + | Crystal structure of 5-Aminolevulinate synthase HemA from Rhodopseudomonas palustris presents multiple conformations.,Zhang T, Chen J, Zheng P, Gong W, Sun J, Liu H Biochem Biophys Res Commun. 2022 Jun 18;609:100-104. doi: , 10.1016/j.bbrc.2022.04.021. Epub 2022 Apr 9. PMID:35427926<ref>PMID:35427926</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7x98" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Rhodopseudomonas palustris]] | ||
| + | [[Category: Liu HP]] | ||
| + | [[Category: Zhang TT]] | ||
Current revision
5-Aminolevulinate synthase HemA from Rhodopseudomonas palustris
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