4bta

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{{STRUCTURE_4bta| PDB=4bta | SCENE= }}
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==CRYSTAL STRUCTURE OF THE PEPTIDE(PRO-PRO-GLY)3 BOUND COMPLEX OF N- TERMINAL DOMAIN AND PEPTIDE SUBSTRATE BINDING DOMAIN OF PROLYL-4 HYDROXYLASE (RESIDUES 1-244) TYPE I FROM HUMAN==
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===CRYSTAL STRUCTURE OF THE PEPTIDE(PRO-PRO-GLY)3 BOUND COMPLEX OF N- TERMINAL DOMAIN AND PEPTIDE SUBSTRATE BINDING DOMAIN OF PROLYL-4 HYDROXYLASE (RESIDUES 1-244) TYPE I FROM HUMAN===
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<StructureSection load='4bta' size='340' side='right' caption='[[4bta]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
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{{ABSTRACT_PUBMED_24207127}}
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== Structural highlights ==
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<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>
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</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>
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<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://www.rcsb.org/pdb/explore.do?structureId=4bta RCSB], [http://www.ebi.ac.uk/pdbsum/4bta PDBsum]</span></td></tr>
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</table>
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<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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==Function==
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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>
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[[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.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[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].
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</div>
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:024207127</ref><references group="xtra"/><references/>
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__TOC__
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</StructureSection>
[[Category: Human]]
[[Category: Human]]
[[Category: Procollagen-proline dioxygenase]]
[[Category: Procollagen-proline dioxygenase]]
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[[Category: Anantharajan, J.]]
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[[Category: Anantharajan, J]]
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[[Category: Koski, M K.]]
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[[Category: Koski, M K]]
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[[Category: Pekkala, M.]]
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[[Category: Pekkala, M]]
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[[Category: Wierenga, R K.]]
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[[Category: Wierenga, R K]]
[[Category: Coiled-coil]]
[[Category: Coiled-coil]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Proline rich peptide]]
[[Category: Proline rich peptide]]
[[Category: Tetratricopeptide repeat motif]]
[[Category: Tetratricopeptide repeat motif]]

Revision as of 09:30, 21 December 2014

CRYSTAL STRUCTURE OF THE PEPTIDE(PRO-PRO-GLY)3 BOUND COMPLEX OF N- TERMINAL DOMAIN AND PEPTIDE SUBSTRATE BINDING DOMAIN OF PROLYL-4 HYDROXYLASE (RESIDUES 1-244) TYPE I FROM HUMAN

4bta, resolution 2.95Å

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