135l

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (15:19, 13 March 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:135l.gif|left|200px]]
 
-
<!--
+
==X-RAY STRUCTURE OF MONOCLINIC TURKEY EGG LYSOZYME AT 1.3 ANGSTROMS RESOLUTION==
-
The line below this paragraph, containing "STRUCTURE_135l", creates the "Structure Box" on the page.
+
<StructureSection load='135l' size='340' side='right'caption='[[135l]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[135l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1lz3 1lz3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=135L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=135L FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</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=135l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=135l OCA], [https://pdbe.org/135l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=135l RCSB], [https://www.ebi.ac.uk/pdbsum/135l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=135l ProSAT]</span></td></tr>
-
{{STRUCTURE_135l| PDB=135l | SCENE= }}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/LYSC_MELGA LYSC_MELGA] 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 ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/35/135l_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=135l ConSurf].
 +
<div style="clear:both"></div>
-
'''X-RAY STRUCTURE OF MONOCLINIC TURKEY EGG LYSOZYME AT 1.3 ANGSTROMS RESOLUTION'''
+
==See Also==
-
 
+
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
-
 
+
__TOC__
-
==Overview==
+
</StructureSection>
-
Monoclinic crystals of turkey egg lysozyme (TEL, E.C. 3.2.1.17) were obtained from 2.2 M ammonium sulfate solution at pH 4.2. They belong to space group P2(1) with unit-cell dimensions a = 38.07, b = 33.20, c = 46.12 A and beta = 110.1 degrees, and contain one molecule in the asymmetric unit (V(m) = 1.91 A(3) Da(-1)). The three-dimensional structure of TEL was solved by the method of multiple isomorphous replacement with anomalous scattering. Area detector data to 1.5 A resolution from native and heavy-atom derivatives were used for the structure determination. The structure was refined by the simulated-annealing method with diffraction data of 10-1.30 A resolution. The conventional R factor was 0.189. The root-mean-square deviations from ideal bond distances and angles were 0.016 A and 2.9 degrees, respectively. The backbone structure of TEL is very similar to that of hen egg lysozyme (HEL) and the difference in seven amino-acid residues does not affect the basic folding of the polypeptide chain. Except for the region from Gly101 to Gly104, the geometry of the active-site cleft is conserved between TEL and HEL. The Gly101 residue is located at the end of the sugar-binding site and the structural change in this region between TEL and HEL is considered to be responsible for the difference in their enzymatic properties.
+
[[Category: Large Structures]]
-
 
+
[[Category: Meleagris gallopavo]]
-
==About this Structure==
+
[[Category: Harata K]]
-
135L is a [[Single protein]] structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1lz3 1lz3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=135L OCA].
+
-
 
+
-
==Reference==
+
-
X-ray structure of monoclinic turkey egg lysozyme at 1.3 A resolution., Harata K, Acta Crystallogr D Biol Crystallogr. 1993 Sep 1;49(Pt 5):497-504. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299509 15299509]
+
-
[[Category: Lysozyme]]
+
-
[[Category: Single protein]]
+
-
[[Category: Harata, K.]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:29:17 2008''
+

Current revision

X-RAY STRUCTURE OF MONOCLINIC TURKEY EGG LYSOZYME AT 1.3 ANGSTROMS RESOLUTION

PDB ID 135l

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/135l"
Personal tools