133l

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Revision as of 06:20, 29 November 2017

ROLE OF ARG 115 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME. X-RAY STRUCTURE OF HIS 115 AND GLU 115 MUTANTS

Structural highlights

133l is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:	Lysozyme, with EC number 3.2.1.17
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[LYSC_HUMAN] Defects in LYZ are a cause of amyloidosis type 8 (AMYL8) [MIM:105200]; also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash.^[1]

Function

[LYSC_HUMAN] 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.

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

The structure of modified human lysozymes (HLs), in which Arg115 is replaced by His or Glu, has been investigated by X-ray analysis at 1.77 A resolution. The mutation of the 115th residue by His does not affect the backbone structure as indicated by a root-mean-square deviation (r.m.s.d) of 0.14 A for the superposition of equivalent C alpha atoms between His115 HL and wild-type HL. In contrast, the corresponding r.m.s.d. value for Glu115 HL is 0.38 A which is twice as large as the estimated co-ordinate error of 0.2 A. Movement of the backbone structure is observed in the region of residues 100 to 130, which give an r.m.s.d. value of 0.61 A and a maximum deviation of 1.46 A for Arg119. A significant movement is also observed in the region of residues 45 to 50, which are located at the opposite side of the region of residues 100 to 120 with respect to the active site cleft. As a result, the active site cleft of Glu115 HL is narrower than the cleft of His115 HL or wild-type HL. This structural change is considered to be responsible for the low catalytic activity of Glu115 HL and the change of the catalytic property found in the hydrolysis of oligosaccharides. The replacement of Arg115 by Glu changes the charge distribution in the molecule, and the change in the electrostatic field may affect polar interactions among residues. The side-chain group of His115 and Glu115 is almost parallel to the indole moiety of Trp34, but the carboxyl group of Glu115 is laterally shifted to avoid overlapping with the indole moiety. The carboxylate anion of Glu115, which does not favor the face-to-face contact with aromatic groups, may provide a driving force for the structural change. The prominent structural change caused by the single mutation suggests that Arg115 is a key residue in maintaining the structure of the active site cleft.

Role of Arg115 in the catalytic action of human lysozyme. X-ray structure of His115 and Glu115 mutants.,Harata K, Muraki M, Jigami Y J Mol Biol. 1993 Oct 5;233(3):524-35. PMID:8105095^[2]

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

References

↑ Pepys MB, Hawkins PN, Booth DR, Vigushin DM, Tennent GA, Soutar AK, Totty N, Nguyen O, Blake CC, Terry CJ, et al.. Human lysozyme gene mutations cause hereditary systemic amyloidosis. Nature. 1993 Apr 8;362(6420):553-7. PMID:8464497 doi:http://dx.doi.org/10.1038/362553a0
↑ Harata K, Muraki M, Jigami Y. Role of Arg115 in the catalytic action of human lysozyme. X-ray structure of His115 and Glu115 mutants. J Mol Biol. 1993 Oct 5;233(3):524-35. PMID:8105095 doi:http://dx.doi.org/10.1006/jmbi.1993.1529

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/133l"

Categories: Human | Lysozyme | Harata, K | Jigami, Y | Muraki, M

@@ Line 3: / Line 3: @@
 <StructureSection load='133l' size='340' side='right' caption='[[133l]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[133l]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=133L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=133L FirstGlance]. <br>
+<table><tr><td colspan='2'>[[133l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=133L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=133L FirstGlance]. <br>
 </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=133l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=133l OCA], [http://pdbe.org/133l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=133l RCSB], [http://www.ebi.ac.uk/pdbsum/133l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=133l ProSAT]</span></td></tr>
@@ Line 37: / Line 37: @@
 __TOC__
 </StructureSection>
+[[Category: Human]]
 [[Category: Lysozyme]]
 [[Category: Harata, K]]
 [[Category: Jigami, Y]]
 [[Category: Muraki, M]]

133l

From Proteopedia

Revision as of 06:20, 29 November 2017

ROLE OF ARG 115 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME. X-RAY STRUCTURE OF HIS 115 AND GLU 115 MUTANTS

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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