4BTB

CRYSTAL STRUCTURE OF THE PEPTIDE(PRO)9 BOUND COMPLEX OF N-TERMINAL DOMAIN AND PEPTIDE SUBSTRATE BINDING DOMAIN OF PROLYL-4 HYDROXYLASE (RESIDUES 1-238) TYPE I FROM HUMAN

Summary for 4BTB

• Entry DOI: 10.2210/pdb4btb/pdb
• Related: 4BT8 4BT9 4BTA
• Descriptor: PROLYL 4-HYDROXYLASE SUBUNIT ALPHA-1, POLY PROLINE PEPTIDE (3 entities in total)
• Functional Keywords: oxidoreductase, tetratricopeptide repeat motif, coiled-coil, proline rich peptide
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Endoplasmic reticulum lumen: P13674
• Total number of polymer chains: 2
• Total formula weight: 28411.13

Authors

Anantharajan, J.,Koski, M.K.,Wierenga, R.K. (deposition date: 2013-06-14, release date: 2013-10-09, Last modification date: 2023-12-20)

Primary citation

Anantharajan, J.,Koski, M.K.,Kursula, P.,Hieta, R.,Bergmann, U.,Myllyharju, J.,Wierenga, R.K.
The Structural Motifs for Substrate Binding and Dimerization of the Alpha Subunit of Collagen Prolyl 4-Hydroxylase
Structure, 21:2107-, 2013

PubMed Abstract: 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 α subunits and two protein disulfide isomerase β subunits. The assembly of these subunits is unknown. The α 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 α 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 α 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.

PubMed: 24207127
DOI: 10.1016/J.STR.2013.09.005

Experimental method

X-RAY DIFFRACTION (1.899 Å)