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1bjr
From Proteopedia
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| - | [[Image:1bjr.gif|left|200px]] | + | [[Image:1bjr.gif|left|200px]] |
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| - | '''COMPLEX FORMED BETWEEN PROTEOLYTICALLY GENERATED LACTOFERRIN FRAGMENT AND PROTEINASE K''' | + | {{Structure |
| + | |PDB= 1bjr |SIZE=350|CAPTION= <scene name='initialview01'>1bjr</scene>, resolution 2.44Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Peptidase_K Peptidase K], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.64 3.4.21.64] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''COMPLEX FORMED BETWEEN PROTEOLYTICALLY GENERATED LACTOFERRIN FRAGMENT AND PROTEINASE K''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BJR is a [ | + | 1BJR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bubalus_bubalis Bubalus bubalis] and [http://en.wikipedia.org/wiki/Engyodontium_album Engyodontium album]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BJR OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of a complex formed between proteolytically-generated lactoferrin fragment and proteinase K., Singh TP, Sharma S, Karthikeyan S, Betzel C, Bhatia KL, Proteins. 1998 Oct 1;33(1):30-8. PMID:[http:// | + | Crystal structure of a complex formed between proteolytically-generated lactoferrin fragment and proteinase K., Singh TP, Sharma S, Karthikeyan S, Betzel C, Bhatia KL, Proteins. 1998 Oct 1;33(1):30-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9741842 9741842] |
[[Category: Bubalus bubalis]] | [[Category: Bubalus bubalis]] | ||
[[Category: Engyodontium album]] | [[Category: Engyodontium album]] | ||
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[[Category: proteinase k]] | [[Category: proteinase k]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:12:06 2008'' |
Revision as of 08:12, 20 March 2008
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| , resolution 2.44Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Peptidase K, with EC number 3.4.21.64 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
COMPLEX FORMED BETWEEN PROTEOLYTICALLY GENERATED LACTOFERRIN FRAGMENT AND PROTEINASE K
Overview
Lactoferrin is an iron binding glycoprotein with a molecular weight of 80 kDa. The molecule is divided into two lobes representing the N-terminal and C-terminal halves of the polypeptide chain, each containing an iron binding site. The serine proteinases such as trypsin, chymotrypsin, and pepsin hydrolyze lactoferrin into two unequal halves while proteinase K divides this protein into two equal halves. In the first step of hydrolysis by proteinase K, the C- and N-lobes, each having a molecular weight of approximately 40 kDa, are generated. In the next step, the lobes are further hydrolyzed into small molecular weight peptides. The proteinase K isolated from the hydrolyzed product does not show enzymatic activity suggesting that the enzyme is inhibited. Furthermore, the hydrolysis experiments on N-lobe and C-lobe showed that the inhibitory fragment came from the C-lobe. The purified lactoferrin fragment was found to be a decapeptide with an amino acid sequence of H2N-Val-Ala-Gln-Gly-Ala-Ala-Gly-Leu-Ala-COOH. The complex formed between proteinase K and lactoferrin fragment was crystallized by microdialysis. The crystals belonged to the monoclinic space group P2(1) with cell dimensions a = 44.4 A, b = 38.6 A, c = 79.2 A, beta = 105.8 degrees and Z = 2. The crystal structure has been determined at 2.4 A resolution. It has been refined to an R factor of 0.163 for 9044 reflections. The Lf-fragment forms several intermolecular interactions with proteinase K. The Ser-224 Ogamma and His-57 N epsilon2 move away to a distance of 3.68 A in the complex. In the crystal structure, Gln-3I (I indicates inhibitor i.e., lactoferrin fragment) is involved in a direct intermolecular interaction with a symmetry related proteinase K molecule through a strong hydrogen bond with Asp-254. The mode of intermolecular interactions in the complex conformational features of the enzyme and placement of the fragment with respect to the enzyme resemble with the molecular complex of proteinase K with its natural inhibitor PKI3 from wheat.
About this Structure
1BJR is a Single protein structure of sequence from Bubalus bubalis and Engyodontium album. Full crystallographic information is available from OCA.
Reference
Crystal structure of a complex formed between proteolytically-generated lactoferrin fragment and proteinase K., Singh TP, Sharma S, Karthikeyan S, Betzel C, Bhatia KL, Proteins. 1998 Oct 1;33(1):30-8. PMID:9741842
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