8dno: Difference between revisions

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-'''Unreleased structure'''
-The entry 8dno is ON HOLD  until Paper Publication
+==Human Brain Aldehyde Dehydrogenase 1 family, member A1==
+<StructureSection load='8dno' size='340' side='right'caption='[[8dno]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8dno]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DNO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DNO FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4&#8491;</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=8dno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dno OCA], [https://pdbe.org/8dno PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dno RCSB], [https://www.ebi.ac.uk/pdbsum/8dno PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dno ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/AL1A1_HUMAN AL1A1_HUMAN] Binds free retinal and cellular retinol-binding protein-bound retinal. Can convert/oxidize retinaldehyde to retinoic acid (By similarity).
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+We recently developed a "Build and Retrieve" cryo-electron microscopy (cryo-EM) methodology, which is capable of simultaneously producing near-atomic resolution cryo-EM maps for several individual proteins from a heterogeneous, multiprotein sample. Here we report the use of "Build and Retrieve" to define the composition of a raw human brain microsomal lysate. From this sample, we simultaneously identify and solve cryo-EM structures of five different brain enzymes whose functions affect neurotransmitter recycling, iron metabolism, glycolysis, axonal development, energy homeostasis, and retinoic acid biosynthesis. Interestingly, malfunction of these important proteins has been directly linked to several neurodegenerative disorders, such as Alzheimer's, Huntington's, and Parkinson's diseases. Our work underscores the importance of cryo-EM in facilitating tissue and organ proteomics at the atomic level.
-Authors: Tringides, M.L.
+A cryo-electron microscopic approach to elucidate protein structures from human brain microsomes.,Tringides ML, Zhang Z, Morgan CE, Su CC, Yu EW Life Sci Alliance. 2022 Nov 30;6(2):e202201724. doi: 10.26508/lsa.202201724. , Print 2023 Feb. PMID:36450447<ref>PMID:36450447</ref>
-Description: Human Brain Aldehyde Dehydrogenase 1 family, member A1
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Tringides, M.L]]
+<div class="pdbe-citations 8dno" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Tringides ML]]