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.


4e3u

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (14:51, 14 March 2024) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
==Crystal Structure of Hen Egg White Lysozyme Cryoprotected in Proline==
==Crystal Structure of Hen Egg White Lysozyme Cryoprotected in Proline==
-
<StructureSection load='4e3u' size='340' side='right' caption='[[4e3u]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
+
<StructureSection load='4e3u' size='340' side='right'caption='[[4e3u]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4e3u]] 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=4E3U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E3U FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4e3u]] 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=4E3U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E3U FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4e3v|4e3v]], [[4e3w|4e3w]], [[4e3x|4e3x]]</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=PRO:PROLINE'>PRO</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'>[https://proteopedia.org/fgij/fg.htm?mol=4e3u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e3u OCA], [https://pdbe.org/4e3u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e3u RCSB], [https://www.ebi.ac.uk/pdbsum/4e3u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e3u ProSAT]</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=4e3u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e3u OCA], [http://pdbe.org/4e3u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4e3u RCSB], [http://www.ebi.ac.uk/pdbsum/4e3u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4e3u ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== 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>
+
[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 ==
+
-
L-Proline is one of Mother Nature's cryoprotectants. Plants and yeast accumulate proline under freeze-induced stress and the use of proline in the cryopreservation of biological samples is well established. Here, it is shown that L-proline is also a useful cryoprotectant for protein crystallography. Proline was used to prepare crystals of lysozyme, xylose isomerase, histidine acid phosphatase and 1-pyrroline-5-carboxylate dehydrogenase for low-temperature data collection. The crystallization solutions in these test cases included the commonly used precipitants ammonium sulfate, sodium chloride and polyethylene glycol and spanned the pH range 4.6-8.5. Thus, proline is compatible with typical protein-crystallization formulations. The proline concentration needed for cryoprotection of these crystals is in the range 2.0-3.0 M. Complete data sets were collected from the proline-protected crystals. Proline performed as well as traditional cryoprotectants based on the diffraction resolution and data-quality statistics. The structures were refined to assess the binding of proline to these proteins. As observed with traditional cryoprotectants such as glycerol and ethylene glycol, the electron-density maps clearly showed the presence of proline molecules bound to the protein. In two cases, histidine acid phosphatase and 1-pyrroline-5-carboxylate dehydrogenase, proline binds in the active site. It is concluded that L-proline is an effective cryoprotectant for protein crystallography.
+
-
 
+
-
Proline: Mother Nature's cryoprotectant applied to protein crystallography.,Pemberton TA, Still BR, Christensen EM, Singh H, Srivastava D, Tanner JJ Acta Crystallogr D Biol Crystallogr. 2012 Aug;68(Pt 8):1010-8. Epub 2012 Jul 17. PMID:22868767<ref>PMID:22868767</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 4e3u" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
Line 27: Line 17:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Chick]]
+
[[Category: Gallus gallus]]
-
[[Category: Lysozyme]]
+
[[Category: Large Structures]]
-
[[Category: Pemberton, T A]]
+
[[Category: Pemberton TA]]
-
[[Category: Tanner, J J]]
+
[[Category: Tanner JJ]]
-
[[Category: Hydrolase]]
+

Current revision

Crystal Structure of Hen Egg White Lysozyme Cryoprotected in Proline

PDB ID 4e3u

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4e3u"
Personal tools