1jug
From Proteopedia
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- | [[Image:1jug.jpg|left|200px]] | + | [[Image:1jug.jpg|left|200px]] |
- | + | ||
- | '''LYSOZYME FROM ECHIDNA MILK (TACHYGLOSSUS ACULEATUS)''' | + | {{Structure |
+ | |PDB= 1jug |SIZE=350|CAPTION= <scene name='initialview01'>1jug</scene>, resolution 1.9Å | ||
+ | |SITE= <scene name='pdbsite=CAB:Ca+Binding+Site'>CAB</scene> | ||
+ | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
+ | |ACTIVITY= [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''LYSOZYME FROM ECHIDNA MILK (TACHYGLOSSUS ACULEATUS)''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1JUG is a [ | + | 1JUG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Tachyglossus_aculeatus Tachyglossus aculeatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JUG OCA]. |
==Reference== | ==Reference== | ||
- | Structure of the calcium-binding echidna milk lysozyme at 1.9 A resolution., Guss JM, Messer M, Costello M, Hardy K, Kumar V, Acta Crystallogr D Biol Crystallogr. 1997 Jul 1;53(Pt 4):355-63. PMID:[http:// | + | Structure of the calcium-binding echidna milk lysozyme at 1.9 A resolution., Guss JM, Messer M, Costello M, Hardy K, Kumar V, Acta Crystallogr D Biol Crystallogr. 1997 Jul 1;53(Pt 4):355-63. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299900 15299900] |
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: lysozyme]] | [[Category: lysozyme]] | ||
- | ''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 12:08:38 2008'' |
Revision as of 10:08, 20 March 2008
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, resolution 1.9Å | |||||||
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Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
LYSOZYME FROM ECHIDNA MILK (TACHYGLOSSUS ACULEATUS)
Overview
A lysozyme isolated from the milk of a monotreme, the echidna, Tachyglossus aculeatus multiaculeatus, has been crystallized (space group P2(1), with unit-cell dimensions a = 37.1, b = 42.0, c = 38.1 A, beta = 91 degrees and Z = 2) and the structure refined to an R value of 0.167 for all measured data in the resolution range 7.0-1.9 A. It had previously been inferred from sequence homology with alpha-lactalbumins that echidna milk lysozyme (EML) would bind one calcium ion per molecule. This has been confirmed in the present study in which the largest peak in a difference Fourier synthesis is associated with a calcium ion. The calcium binding site of EML is very similar to that observed in baboon and human alpha-lactalbumins, and in a human lysozyme engineered to contain a calcium-binding site. The overall fold of the protein is similar to that of chick-type lysozymes. EML, like pigeon lysozyme, has only 125 residues terminating at a cysteine but in EML this forms a disulfide with a cysteine at residue 9 whereas the equivalent cysteine residue in all other lysozymes of known sequence occurs at position 6. These changes cause some minor structural rearrangements. The binding of calcium appears to have had little effect on the polypeptide backbone conformation and caused only small changes in the conformation of side chains coordinating the calcium ion. A homology modelling study [Acharya, Stuart, Phillips, McKenzie & Teahan (1994). J. Protein Chem. 13(6), 569-584] correctly predicted the overall structure of EML and the nature of its calcium binding site but generally failed to model some more subtle differences observed in the EML structure as evidenced by the fact that the homology model more closely resembles the starting structure from which the model was derived than it does the crystal structure.
About this Structure
1JUG is a Single protein structure of sequence from Tachyglossus aculeatus. Full crystallographic information is available from OCA.
Reference
Structure of the calcium-binding echidna milk lysozyme at 1.9 A resolution., Guss JM, Messer M, Costello M, Hardy K, Kumar V, Acta Crystallogr D Biol Crystallogr. 1997 Jul 1;53(Pt 4):355-63. PMID:15299900
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