3ajn

From Proteopedia

(Difference between revisions)

Revision as of 10:42, 25 December 2014

Structural basis of glycine amide on suppression of protein aggregation by high resolution X-ray analysis

Structural highlights

3ajn is a 1 chain structure with sequence from Gallus gallus. This structure supersedes the now removed PDB entry 2zxs. 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, RCSB, PDBsum

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]

Publication Abstract from PubMed

Glycine amide (GlyAd), a typically amidated amino acid, is a versatile additive that suppresses protein aggregation during refolding, heat treatment, and crystallization. In spite of its effectiveness, the exact mechanism by which GlyAd suppresses protein aggregation remains to be elucidated. Here, we show the crystal structure of the GlyAd-lysozyme complex by high resolution X-ray crystallographic analysis at a 1.05A resolution. GlyAd bound to the lysozyme surface near aromatic residues and decreased the amount of bound waters and increased the mobility of protein. Arg and GlyAd molecules are different in binding sites and patterns from glycerol and related compounds, indicating that decreasing hydrophobic patches might be involved in suppression of protein aggregation.

Glycine amide shielding on the aromatic surfaces of lysozyme: Implication for suppression of protein aggregation.,Ito L, Shiraki K, Makino M, Hasegawa K, Kumasaka T FEBS Lett. 2011 Feb 4;585(3):555-60. Epub 2011 Jan 14. PMID:21237160^[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
↑ Ito L, Shiraki K, Makino M, Hasegawa K, Kumasaka T. Glycine amide shielding on the aromatic surfaces of lysozyme: Implication for suppression of protein aggregation. FEBS Lett. 2011 Feb 4;585(3):555-60. Epub 2011 Jan 14. PMID:21237160 doi:10.1016/j.febslet.2011.01.008

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3ajn"

@@ Line 7: / Line 7: @@
 <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=3ajn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ajn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ajn RCSB], [http://www.ebi.ac.uk/pdbsum/3ajn PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/LYSC_CHICK 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.<ref>PMID:22044478</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 26: @@
 [[Category: Gallus gallus]]
 [[Category: Lysozyme]]
-[[Category: Hasegawa, K.]]
+[[Category: Hasegawa, K]]
-[[Category: Ito, L.]]
+[[Category: Ito, L]]
-[[Category: Kumasaka, T.]]
+[[Category: Kumasaka, T]]
-[[Category: Shiraki, K.]]
+[[Category: Shiraki, K]]
 [[Category: Glycine amide]]
 [[Category: Glycosidase]]
 [[Category: Hydrolase]]
-[[Category: Lysozyme]]

3ajn

From Proteopedia

Revision as of 10:42, 25 December 2014

Structural basis of glycine amide on suppression of protein aggregation by high resolution X-ray analysis

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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