2yq8
From Proteopedia
(Difference between revisions)
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| - | + | ==Crystal structure of the SeMet-labeled N-terminal domain and peptide substrate binding domain of alpha subunit of prolyl-4 hydroxylase type I from human.== | |
| - | + | <StructureSection load='2yq8' size='340' side='right' caption='[[2yq8]], [[Resolution|resolution]] 2.99Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[2yq8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YQ8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YQ8 FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Procollagen-proline_dioxygenase Procollagen-proline dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.2 1.14.11.2] </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=2yq8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yq8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2yq8 RCSB], [http://www.ebi.ac.uk/pdbsum/2yq8 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Procollagen-proline dioxygenase]] | [[Category: Procollagen-proline dioxygenase]] | ||
| - | [[Category: Anantharajan, J | + | [[Category: Anantharajan, J]] |
| - | [[Category: Koski, M K | + | [[Category: Koski, M K]] |
| - | [[Category: Wierenga, R K | + | [[Category: Wierenga, R K]] |
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
Revision as of 18:09, 21 December 2014
Crystal structure of the SeMet-labeled N-terminal domain and peptide substrate binding domain of alpha subunit of prolyl-4 hydroxylase type I from human.
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