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| <StructureSection load='4bta' size='340' side='right'caption='[[4bta]], [[Resolution|resolution]] 2.95Å' scene=''> | | <StructureSection load='4bta' size='340' side='right'caption='[[4bta]], [[Resolution|resolution]] 2.95Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[4bta]] is a 3 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=4BTA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BTA FirstGlance]. <br> | | <table><tr><td colspan='2'>[[4bta]] is a 3 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=4BTA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BTA FirstGlance]. <br> |
| </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bt8|4bt8]], [[4bt9|4bt9]], [[4btb|4btb]]</td></tr> | | </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=4bta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bta OCA], [https://pdbe.org/4bta PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bta RCSB], [https://www.ebi.ac.uk/pdbsum/4bta PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bta ProSAT]</span></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>
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| <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=4bta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bta OCA], [http://pdbe.org/4bta PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bta RCSB], [http://www.ebi.ac.uk/pdbsum/4bta PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bta ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://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;">
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| == Publication Abstract from PubMed ==
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| 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.
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| 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>
| | ==See Also== |
| | | *[[Hydroxylases 3D structures|Hydroxylases 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 4bta" style="background-color:#fffaf0;"></div>
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| == References == | |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Human]] | | [[Category: Homo sapiens]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Procollagen-proline dioxygenase]]
| | [[Category: Anantharajan J]] |
| [[Category: Anantharajan, J]] | | [[Category: Koski MK]] |
| [[Category: Koski, M K]] | | [[Category: Pekkala M]] |
| [[Category: Pekkala, M]] | | [[Category: Wierenga RK]] |
| [[Category: Wierenga, R K]] | |
| [[Category: Coiled-coil]]
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| [[Category: Oxidoreductase]]
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| [[Category: Proline rich peptide]]
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| [[Category: Tetratricopeptide repeat motif]]
| |