6ax7: Difference between revisions

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-'''Unreleased structure'''
-The entry 6ax7 is ON HOLD  until Sep 06 2019
+==The crystal structure of a lysyl hydroxylase from Acanthamoeba polyphaga mimivirus==
+<StructureSection load='6ax7' size='340' side='right' caption='[[6ax7]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6ax7]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AX7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AX7 FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.4 1.14.11.4] </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=6ax7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ax7 OCA], [http://pdbe.org/6ax7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ax7 RCSB], [http://www.ebi.ac.uk/pdbsum/6ax7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ax7 ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Collagen lysyl hydroxylases (LH1-3) are Fe(2+)- and 2-oxoglutarate (2-OG)-dependent oxygenases that maintain extracellular matrix homeostasis. High LH2 levels cause stable collagen cross-link accumulations that promote fibrosis and cancer progression. However, developing LH antagonists will require structural insights. Here, we report a 2 A crystal structure and X-ray scattering on dimer assemblies for the LH domain of L230 in Acanthamoeba polyphaga mimivirus. Loop residues in the double-stranded beta-helix core generate a tail-to-tail dimer. A stabilizing hydrophobic leucine locks into an aromatic tyrosine-pocket on the opposite subunit. An active site triad coordinates Fe(2+). The two active sites flank a deep surface cleft that suggest dimerization creates a collagen-binding site. Loss of Fe(2+)-binding disrupts the dimer. Dimer disruption and charge reversal in the cleft increase Km and reduce LH activity. Ectopic L230 expression in tumors promotes collagen cross-linking and metastasis. These insights suggest inhibitor targets for fibrosis and cancer.
-Authors:
+Pro-metastatic collagen lysyl hydroxylase dimer assemblies stabilized by Fe(2+)-binding.,Guo HF, Tsai CL, Terajima M, Tan X, Banerjee P, Miller MD, Liu X, Yu J, Byemerwa J, Alvarado S, Kaoud TS, Dalby KN, Bota-Rabassedas N, Chen Y, Yamauchi M, Tainer JA, Phillips GN Jr., Kurie JM Nat Commun. 2018 Feb 6;9(1):512. doi: 10.1038/s41467-018-02859-z. PMID:29410444<ref>PMID:29410444</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6ax7" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Oxidoreductase]]
+[[Category: Alvarado, S]]
+[[Category: Guo, H]]
+[[Category: Kurie, J M]]
+[[Category: Miller, M D]]
+[[Category: Phillips, G N]]
+[[Category: Tainer, J A]]
+[[Category: Tsai, C]]
+[[Category: Collagen]]
+[[Category: Dimer]]
+[[Category: Dioxygenase]]
+[[Category: Double-stranded ?-helix]]