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{{STRUCTURE_4b4j|  PDB=4b4j  |  SCENE=  }}
===1.25 A Structure of Lysozyme Crystallized with (RS)-2-methyl-2,4- pentanediol===


==Function==
==1.25 A Structure of Lysozyme Crystallized with (RS)-2-methyl-2,4- pentanediol==
[[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>  
<StructureSection load='4b4j' size='340' side='right'caption='[[4b4j]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4b4j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B4J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B4J FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.25&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4b4j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b4j OCA], [https://pdbe.org/4b4j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b4j RCSB], [https://www.ebi.ac.uk/pdbsum/4b4j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b4j ProSAT]</span></td></tr>
</table>
== Function ==
[https://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 ==
Chiral control of crystallization has ample precedent in the small-molecule world, but relatively little is known about the role of chirality in protein crystallization. In this study, lysozyme was crystallized in the presence of the chiral additive 2-methyl-2,4-pentanediol (MPD) separately using the R and S enantiomers as well as with a racemic RS mixture. Crystals grown with (R)-MPD had the most order and produced the highest resolution protein structures. This result is consistent with the observation that in the crystals grown with (R)-MPD and (RS)-MPD the crystal contacts are made by (R)-MPD, demonstrating that there is preferential interaction between lysozyme and this enantiomer. These findings suggest that chiral interactions are important in protein crystallization.


==About this Structure==
Crystallization of lysozyme with (R)-, (S)- and (RS)-2-methyl-2,4-pentanediol.,Stauber M, Jakoncic J, Berger J, Karp JM, Axelbaum A, Sastow D, Buldyrev SV, Hrnjez BJ, Asherie N Acta Crystallogr D Biol Crystallogr. 2015 Mar 1;71(Pt 3):427-41. doi:, 10.1107/S1399004714025061. Epub 2015 Feb 26. PMID:25760593<ref>PMID:25760593</ref>
[[4b4j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B4J OCA].
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4b4j" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Hen Egg-White (HEW) Lysozyme|Hen Egg-White (HEW) Lysozyme]]
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
 
== References ==
==Reference==
<references/>
<references group="xtra"/><references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Lysozyme]]
[[Category: Large Structures]]
[[Category: Asherie, N.]]
[[Category: Asherie N]]
[[Category: Axelbaum, A.]]
[[Category: Axelbaum A]]
[[Category: Berger, J.]]
[[Category: Berger J]]
[[Category: Jakoncic, J.]]
[[Category: Jakoncic J]]
[[Category: Stauber, M.]]
[[Category: Stauber M]]
[[Category: Chirality]]
[[Category: Hydrolase]]

Latest revision as of 13:40, 6 November 2024

1.25 A Structure of Lysozyme Crystallized with (RS)-2-methyl-2,4- pentanediol1.25 A Structure of Lysozyme Crystallized with (RS)-2-methyl-2,4- pentanediol

Structural highlights

4b4j is a 1 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.25Å
Ligands:,
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]

Publication Abstract from PubMed

Chiral control of crystallization has ample precedent in the small-molecule world, but relatively little is known about the role of chirality in protein crystallization. In this study, lysozyme was crystallized in the presence of the chiral additive 2-methyl-2,4-pentanediol (MPD) separately using the R and S enantiomers as well as with a racemic RS mixture. Crystals grown with (R)-MPD had the most order and produced the highest resolution protein structures. This result is consistent with the observation that in the crystals grown with (R)-MPD and (RS)-MPD the crystal contacts are made by (R)-MPD, demonstrating that there is preferential interaction between lysozyme and this enantiomer. These findings suggest that chiral interactions are important in protein crystallization.

Crystallization of lysozyme with (R)-, (S)- and (RS)-2-methyl-2,4-pentanediol.,Stauber M, Jakoncic J, Berger J, Karp JM, Axelbaum A, Sastow D, Buldyrev SV, Hrnjez BJ, Asherie N Acta Crystallogr D Biol Crystallogr. 2015 Mar 1;71(Pt 3):427-41. doi:, 10.1107/S1399004714025061. Epub 2015 Feb 26. PMID:25760593[2]

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

See Also

References

  1. 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
  2. Stauber M, Jakoncic J, Berger J, Karp JM, Axelbaum A, Sastow D, Buldyrev SV, Hrnjez BJ, Asherie N. Crystallization of lysozyme with (R)-, (S)- and (RS)-2-methyl-2,4-pentanediol. Acta Crystallogr D Biol Crystallogr. 2015 Mar 1;71(Pt 3):427-41. doi:, 10.1107/S1399004714025061. Epub 2015 Feb 26. PMID:25760593 doi:http://dx.doi.org/10.1107/S1399004714025061

4b4j, resolution 1.25Å

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