1ckg: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1ckg.jpg|left|200px]] | [[Image:1ckg.jpg|left|200px]] | ||
'''T52V MUTANT HUMAN LYSOZYME''' | {{Structure | ||
|PDB= 1ckg |SIZE=350|CAPTION= <scene name='initialview01'>1ckg</scene>, resolution 2.2Å | |||
|SITE= | |||
|LIGAND= | |||
|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= | |||
}} | |||
'''T52V MUTANT HUMAN LYSOZYME''' | |||
==Overview== | ==Overview== | ||
| Line 10: | Line 19: | ||
==About this Structure== | ==About this Structure== | ||
1CKG is a [ | 1CKG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CKG OCA]. | ||
==Reference== | ==Reference== | ||
Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,)., Takano K, Yamagata Y, Funahashi J, Hioki Y, Kuramitsu S, Yutani K, Biochemistry. 1999 Sep 28;38(39):12698-708. PMID:[http:// | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,)., Takano K, Yamagata Y, Funahashi J, Hioki Y, Kuramitsu S, Yutani K, Biochemistry. 1999 Sep 28;38(39):12698-708. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10504240 10504240] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
| Line 24: | Line 33: | ||
[[Category: stability]] | [[Category: stability]] | ||
''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 10:25:29 2008'' | ||
Revision as of 11:25, 20 March 2008
| |||||||
| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
T52V MUTANT HUMAN LYSOZYME
OverviewOverview
In globular proteins, there are intermolecular hydrogen bonds between protein and water molecules, and between water molecules, which are bound with the proteins, in addition to intramolecular hydrogen bonds. To estimate the contribution of these hydrogen bonds to the conformational stability of a protein, the thermodynamic parameters for denaturation and the crystal structures of five Thr to Val and five Thr to Ala mutant human lysozymes were determined. The denaturation Gibbs energy (DeltaG) of Thr to Val and Thr to Ala mutant proteins was changed from 4.0 to -5.6 kJ/mol and from 1.6 to -6.3 kJ/mol, respectively, compared with that of the wild-type protein. The contribution of hydrogen bonds to the stability (DeltaDeltaG(HB)) of the Thr and other mutant human lysozymes previously reported was extracted from the observed stability changes (DeltaDeltaG) with correction for changes in hydrophobicity and side chain conformational entropy between the wild-type and mutant structures. The estimation of the DeltaDeltaG(HB) values of all mutant proteins after removal of hydrogen bonds, including protein-water hydrogen bonds, indicates a favorable contribution of the intra- and intermolecular hydrogen bonds to the protein stability. The net contribution of an intramolecular hydrogen bond (DeltaG(HB[pp])), an intermolecular one between protein and ordered water molecules (DeltaG(HB[pw])), and an intermolecular one between ordered water molecules (DeltaG(HB[ww])) could be estimated to be 8. 5, 5.2, and 5.0 kJ/mol, respectively, for a 3 A long hydrogen bond. This result shows the different contributions to protein stability of intra- and intermolecular hydrogen bonds. The entropic cost due to the introduction of a water molecule (DeltaG(H)()2(O)) could be also estimated to be about 8 kJ/mol.
DiseaseDisease
Known diseases associated with this structure: Amyloidosis, renal OMIM:[153450], Microphthalmia, syndromic 1 OMIM:[309800]
About this StructureAbout this Structure
1CKG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,)., Takano K, Yamagata Y, Funahashi J, Hioki Y, Kuramitsu S, Yutani K, Biochemistry. 1999 Sep 28;38(39):12698-708. PMID:10504240
Page seeded by OCA on Thu Mar 20 10:25:29 2008