1gwd

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (00:01, 21 November 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1gwd.jpg|left|200px]]
 
-
{{Structure
+
==Tri-iodide derivative of hen egg-white lysozyme==
-
|PDB= 1gwd |SIZE=350|CAPTION= <scene name='initialview01'>1gwd</scene>, resolution 1.77&Aring;
+
<StructureSection load='1gwd' size='340' side='right'caption='[[1gwd]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
-
|SITE= <scene name='pdbsite=EA1:Egl+Binding+Site+For+Chain+A'>EA1</scene>
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>
+
<table><tr><td colspan='2'>[[1gwd]] 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=1GWD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GWD FirstGlance]. <br>
-
|ACTIVITY= <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.77&#8491;</td></tr>
-
|GENE=
+
<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=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-
|DOMAIN=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gwd OCA], [https://pdbe.org/1gwd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gwd RCSB], [https://www.ebi.ac.uk/pdbsum/1gwd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gwd ProSAT]</span></td></tr>
-
|RELATEDENTRY=
+
</table>
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gwd OCA], [http://www.ebi.ac.uk/pdbsum/1gwd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gwd RCSB]</span>
+
== 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/gw/1gwd_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1gwd ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
A series of experiments performed at Cu Kalpha wavelength on in-house X-ray equipment are presented which investigate two possibilities for enhancing the experimental phasing signal by means of (i) triiodide/iodide soaks using KI/I(2) and (ii) combinations of counter-ions introduced using the short cryosoak method. Triiodide-derivative crystal structures for five test proteins have been refined and reveal that iodine can bind as polyiodide and single iodide ions through hydrophobic and hydrogen-bonding interactions both at the molecular surface and in intramolecular and intermolecular cavities. In three cases, the structures could be automatically determined with autoSHARP using in-house SAD and SIRAS data. The investigation of combinatorial counter-ion replacement using multiple salts with Na(+) and Cs(+) as cations and I(-) and Cl(-) as anions reveals that, for the case of hen egg-white lysozyme, significant improvement in phasing signal is obtained by the combined use of salts compared with SIRAS methods using native and single short-soak derivative data sets.
-
'''TRI-IODIDE DERIVATIVE OF HEN EGG-WHITE LYSOZYME'''
+
Triiodide derivatization and combinatorial counter-ion replacement: two methods for enhancing phasing signal using laboratory Cu Kalpha X-ray equipment.,Evans G, Bricogne G Acta Crystallogr D Biol Crystallogr. 2002 Jun;58(Pt 6 Pt 2):976-91. Epub, 2002 May 29. PMID:12037300<ref>PMID:12037300</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1gwd" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
A series of experiments performed at Cu Kalpha wavelength on in-house X-ray equipment are presented which investigate two possibilities for enhancing the experimental phasing signal by means of (i) triiodide/iodide soaks using KI/I(2) and (ii) combinations of counter-ions introduced using the short cryosoak method. Triiodide-derivative crystal structures for five test proteins have been refined and reveal that iodine can bind as polyiodide and single iodide ions through hydrophobic and hydrogen-bonding interactions both at the molecular surface and in intramolecular and intermolecular cavities. In three cases, the structures could be automatically determined with autoSHARP using in-house SAD and SIRAS data. The investigation of combinatorial counter-ion replacement using multiple salts with Na(+) and Cs(+) as cations and I(-) and Cl(-) as anions reveals that, for the case of hen egg-white lysozyme, significant improvement in phasing signal is obtained by the combined use of salts compared with SIRAS methods using native and single short-soak derivative data sets.
+
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
1GWD is a [[Single protein]] structure of 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=1GWD OCA].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
-
Triiodide derivatization and combinatorial counter-ion replacement: two methods for enhancing phasing signal using laboratory Cu Kalpha X-ray equipment., Evans G, Bricogne G, Acta Crystallogr D Biol Crystallogr. 2002 Jun;58(Pt 6 Pt 2):976-91. Epub, 2002 May 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12037300 12037300]
+
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
-
[[Category: Lysozyme]]
+
[[Category: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: Bricogne G]]
-
[[Category: Bricogne, G.]]
+
[[Category: Evans G]]
-
[[Category: Evans, G.]]
+
-
[[Category: aller]]
+
-
[[Category: bacteriolytic enzyme]]
+
-
[[Category: glycosidase]]
+
-
[[Category: hydrolase]]
+
-
[[Category: signal]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:52:40 2008''
+

Current revision

Tri-iodide derivative of hen egg-white lysozyme

PDB ID 1gwd

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools