This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

3lhm

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 07:15, 29 November 2017

CRYSTAL STRUCTURES OF THE APO-AND HOLOMUTANT HUMAN LYSOZYMES WITH AN INTRODUCED CA2+ BINDING SITE

Structural highlights

3lhm 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.
Ligands:
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 three-dimensional structures of apo- and holomutant human lysozymes (D86/92 lysozyme), in which a calcium binding site was designed and created for enhancing molecular stability by replacing both Gln86 and Ala92 with aspartic acids, were refined at 1.8-A resolution by x-ray crystallography. The overall structures and crystallographic thermal factors of all three proteins, the apo-, holo-D86/92, and the wild-type human lysozymes, were essentially identical; these results showed that the introduction of the calcium binding site did not affect either the overall structure or molecular rigidity of the proteins. However, structure analyses of the apo-D86/92 lysozyme revealed that the mutations affected the side chain conformation of residue 86 and hydrogen networks between the protein and the internal solvent molecules. In the structure of the holo-D86/92 lysozyme, seven oxygen ligands formed a slightly distorted pentagonal bipyramid around the calcium ion, indicating that the coordination around the calcium ion was quite similar to that in baboon alpha-lactalbumin. The pentagonal bipyramid coordination could be one of the most widely found and appropriate calcium binding schemes in proteins.

Crystal structures of the apo- and holomutant human lysozymes with an introduced Ca2+ binding site.,Inaka K, Kuroki R, Kikuchi M, Matsushima M J Biol Chem. 1991 Nov 5;266(31):20666-71. PMID:1939116^[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
↑ Inaka K, Kuroki R, Kikuchi M, Matsushima M. Crystal structures of the apo- and holomutant human lysozymes with an introduced Ca2+ binding site. J Biol Chem. 1991 Nov 5;266(31):20666-71. PMID:1939116

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/3lhm"

Categories: Human | Lysozyme | Inaka, K | Matsushima, M

@@ Line 1: / Line 1: @@
 ==CRYSTAL STRUCTURES OF THE APO-AND HOLOMUTANT HUMAN LYSOZYMES WITH AN INTRODUCED CA2+ BINDING SITE==
 <StructureSection load='3lhm' size='340' side='right' caption='[[3lhm]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=3lhm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lhm OCA], [http://pdbe.org/3lhm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lhm RCSB], [http://www.ebi.ac.uk/pdbsum/3lhm PDBsum]</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=3lhm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lhm OCA], [http://pdbe.org/3lhm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lhm RCSB], [http://www.ebi.ac.uk/pdbsum/3lhm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lhm ProSAT]</span></td></tr>
 </table>
 == Disease ==

3lhm

From Proteopedia

Revision as of 07:15, 29 November 2017

CRYSTAL STRUCTURES OF THE APO-AND HOLOMUTANT HUMAN LYSOZYMES WITH AN INTRODUCED CA2+ BINDING SITE

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox