1tjc
From Proteopedia
(New page: 200px<br /> <applet load="1tjc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tjc, resolution 2.30Å" /> '''Crystal structure o...) |
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caption="1tjc, resolution 2.30Å" /> | caption="1tjc, resolution 2.30Å" /> | ||
'''Crystal structure of peptide-substrate-binding domain of human type I collagen prolyl 4-hydroxylase'''<br /> | '''Crystal structure of peptide-substrate-binding domain of human type I collagen prolyl 4-hydroxylase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Collagen prolyl 4-hydroxylases catalyze the formation of 4-hydroxyproline | + | Collagen prolyl 4-hydroxylases catalyze the formation of 4-hydroxyproline in -X-Pro-Gly-sequences and have an essential role in collagen synthesis. The vertebrate enzymes are alpha2beta2 tetramers in which the catalytic alpha-subunits contain separate peptide-substrate-binding and catalytic domains. We report on the crystal structure of the peptide-substrate-binding domain of the human type I enzyme refined at 2.3 A resolution. It was found to belong to a family of tetratricopeptide repeat domains that are involved in many protein-protein interactions and consist of five alpha-helices forming two tetratricopeptide repeat motifs plus the solvating helix. A prominent feature of its concave surface is a deep groove lined by tyrosines, a putative binding site for proline-rich Tripeptides. Solvent-exposed side chains of three of the tyrosines have a repeat distance similar to that of a poly-L-proline type II helix. The aromatic surface ends at one of the tyrosines, where the groove curves almost 90 degrees away from the linear arrangement of the three tyrosine side chains, possibly inducing a bent conformation in the bound peptide. This finding is consistent with previous suggestions by others that a minimal structural requirement for proline 4-hydroxylation may be a sequence in the poly-L-proline type II conformation followed by a beta-turn in the Pro-Gly segment. Site-directed mutagenesis indicated that none of the tyrosines was critical for tetramer assembly, whereas most of them were critical for the binding of a peptide substrate and inhibitor both to the domain and the alpha2beta2 enzyme tetramer. |
==About this Structure== | ==About this Structure== | ||
| - | 1TJC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [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] Full crystallographic information is available from [http:// | + | 1TJC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TJC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bergmann, U.]] | [[Category: Bergmann, U.]] | ||
[[Category: Hieta, R.]] | [[Category: Hieta, R.]] | ||
| - | [[Category: Kivirikko, K | + | [[Category: Kivirikko, K I.]] |
[[Category: Myllyharju, J.]] | [[Category: Myllyharju, J.]] | ||
[[Category: Pekkala, M.]] | [[Category: Pekkala, M.]] | ||
| - | [[Category: Wierenga, R | + | [[Category: Wierenga, R K.]] |
[[Category: helical bundle]] | [[Category: helical bundle]] | ||
[[Category: tpr]] | [[Category: tpr]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:14:06 2008'' |
Revision as of 13:14, 21 February 2008
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Crystal structure of peptide-substrate-binding domain of human type I collagen prolyl 4-hydroxylase
Overview
Collagen prolyl 4-hydroxylases catalyze the formation of 4-hydroxyproline in -X-Pro-Gly-sequences and have an essential role in collagen synthesis. The vertebrate enzymes are alpha2beta2 tetramers in which the catalytic alpha-subunits contain separate peptide-substrate-binding and catalytic domains. We report on the crystal structure of the peptide-substrate-binding domain of the human type I enzyme refined at 2.3 A resolution. It was found to belong to a family of tetratricopeptide repeat domains that are involved in many protein-protein interactions and consist of five alpha-helices forming two tetratricopeptide repeat motifs plus the solvating helix. A prominent feature of its concave surface is a deep groove lined by tyrosines, a putative binding site for proline-rich Tripeptides. Solvent-exposed side chains of three of the tyrosines have a repeat distance similar to that of a poly-L-proline type II helix. The aromatic surface ends at one of the tyrosines, where the groove curves almost 90 degrees away from the linear arrangement of the three tyrosine side chains, possibly inducing a bent conformation in the bound peptide. This finding is consistent with previous suggestions by others that a minimal structural requirement for proline 4-hydroxylation may be a sequence in the poly-L-proline type II conformation followed by a beta-turn in the Pro-Gly segment. Site-directed mutagenesis indicated that none of the tyrosines was critical for tetramer assembly, whereas most of them were critical for the binding of a peptide substrate and inhibitor both to the domain and the alpha2beta2 enzyme tetramer.
About this Structure
1TJC is a Single protein structure of sequence from Homo sapiens. Active as Procollagen-proline dioxygenase, with EC number 1.14.11.2 Full crystallographic information is available from OCA.
Reference
The peptide-substrate-binding domain of collagen prolyl 4-hydroxylases is a tetratricopeptide repeat domain with functional aromatic residues., Pekkala M, Hieta R, Bergmann U, Kivirikko KI, Wierenga RK, Myllyharju J, J Biol Chem. 2004 Dec 10;279(50):52255-61. Epub 2004 Sep 28. PMID:15456751
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