4bt9: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[4bt9]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BT9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BT9 FirstGlance]. <br>
-</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=4bt9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bt9 OCA], [https://pdbe.org/4bt9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bt9 RCSB], [https://www.ebi.ac.uk/pdbsum/4bt9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bt9 ProSAT]</span></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]] 1.9&#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=4bt9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bt9 OCA], [https://pdbe.org/4bt9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bt9 RCSB], [https://www.ebi.ac.uk/pdbsum/4bt9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bt9 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/P4HA1_HUMAN P4HA1_HUMAN]] Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
+[https://www.uniprot.org/uniprot/P4HA1_HUMAN P4HA1_HUMAN] Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Collagen prolyl 4-hydroxylase (C-P4H) catalyzes the proline hydroxylation of procollagen, an essential modification in the maturation of collagens. C-P4H consists of two catalytic alpha subunits and two protein disulfide isomerase beta subunits. The assembly of these subunits is unknown. The alpha subunit contains an N domain (1-143), a peptide-substrate-binding-domain (PSB, 144-244) and a catalytic domain (245-517). Here, we report the dimeric structure of the N-terminal region (1-244) of the alpha subunit. It is shown that the N domain has an important role in the assembly of the C-P4H tetramer, by forming an extended four-helix bundle that includes an antiparallel coiled-coil dimerization motif between the two alpha subunits. Complexes of this construct with a C-P4H inhibitor and substrate show the mode of peptide-binding to the PSB domain. Both peptides adopt a poly-(L)-proline-type-II helix conformation and bind in a curved, asymmetric groove lined by conserved tyrosines and an Arg-Asp salt bridge.
+The Structural Motifs for Substrate Binding and Dimerization of the alpha Subunit of Collagen Prolyl 4-Hydroxylase.,Anantharajan J, Koski MK, Kursula P, Hieta R, Bergmann U, Myllyharju J, Wierenga RK Structure. 2013 Oct 23. pii: S0969-2126(13)00355-9. doi:, 10.1016/j.str.2013.09.005. PMID:24207127<ref>PMID:24207127</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4bt9" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Hydroxylases 3D structures|Hydroxylases 3D structures]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>