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1ios

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Revision as of 10:35, 30 October 2019

STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLING MUTATION

Structural highlights

1ios is a 1 chain structure with sequence from Chick. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1ioq, 1ior, 1iot
Activity:	Lysozyme, with EC number 3.2.1.17
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Stabilization of a protein using cavity-filling strategy has hardly been successful because of unfavorable van der Waals contacts. We succeeded in stabilizing lysozymes by cavity-filling mutations. The mutations were checked by a simple energy minimization in advance. It was shown clearly that the sum of free energy change caused by the hydrophobicity and the cavity size was correlated very well with protein stability. We also considered the aromatic-aromatic interaction. It is reconfirmed that the cavity-filling mutation in a hydrophobic core is a very useful method to stabilize a protein when the mutation candidate is selected carefully.

Stabilization of hen egg white lysozyme by a cavity-filling mutation.,Ohmura T, Ueda T, Ootsuka K, Saito M, Imoto T Protein Sci. 2001 Feb;10(2):313-20. PMID:11266617^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Maehashi K, Matano M, Irisawa T, Uchino M, Kashiwagi Y, Watanabe T. Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white. Gene. 2012 Jan 15;492(1):244-9. doi: 10.1016/j.gene.2011.10.021. Epub 2011 Oct, 25. PMID:22044478 doi:10.1016/j.gene.2011.10.021
↑ Ohmura T, Ueda T, Ootsuka K, Saito M, Imoto T. Stabilization of hen egg white lysozyme by a cavity-filling mutation. Protein Sci. 2001 Feb;10(2):313-20. PMID:11266617

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ios"

@@ Line 1: / Line 1: @@
 ==STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLING MUTATION==
-<StructureSection load='1ios' size='340' side='right' caption='[[1ios]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
+<StructureSection load='1ios' size='340' side='right'caption='[[1ios]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1ios]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IOS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IOS FirstGlance]. <br>
@@ Line 37: / Line 37: @@
 </StructureSection>
 [[Category: Chick]]
+[[Category: Large Structures]]
 [[Category: Lysozyme]]
 [[Category: Imoto, T]]

1ios

From Proteopedia

Revision as of 10:35, 30 October 2019

STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLING MUTATION

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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