3m0u: Difference between revisions

Line 3:

== Structural highlights ==

<table><tr><td colspan='2'>[[3m0u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Chick Chick~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M0U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M0U FirstGlance]. <br>

<table><tr><td colspan='2'>[[3m0u]] 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=3M0U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M0U FirstGlance]. <br>

</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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]] 1.1Å</td></tr>

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr>

~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene|Gene~~:~~]]</b~~></~~td><td class="sblockDat"~~>~~SPTAN1, SPTA2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK])~~</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=3m0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m0u OCA], [https://pdbe.org/3m0u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m0u RCSB], [https://www.ebi.ac.uk/pdbsum/3m0u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m0u ProSAT]</span></td></tr>

</table>

== Function ==

[[https://www.uniprot.org/uniprot/SPTN1_CHICK SPTN1_CHICK]] Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization.

[https://www.uniprot.org/uniprot/SPTN1_CHICK SPTN1_CHICK] Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization.

~~<div style="background-color:#fffaf0;">~~

~~== Publication Abstract from PubMed ==~~

alpha-Spectrin SH3-domain (Spc-SH3) crystallization is characterized by very fast growth of the crystals in the presence of ammonium sulfate as a precipitant agent. The origin of this behaviour can be attributed to the presence of a proline residue that participates in a crystal contact mimicking the binding of proline-rich sequences to SH3 domains. This residue, Pro20, is located in the RT loop and is the main contact in one of the interfaces present in the orthorhombic Spc-SH3 crystal structures. In order to understand the molecular interactions that are responsible for the very fast crystal growth of the wild-type (WT) Spc-SH3 crystals, the crystal structure of a triple mutant in which the residues Ser19-Pro20-Arg21 in the RT loop have been replaced by Gly19-Asp20-Ser21 (GDS Spc-SH3 mutant) has been solved. The removal of the critical proline residue results in slower nucleation of the Spc-SH3 crystals and a different arrangement of the protein molecules in the unit cell, leading to a crystal that belongs to the tetragonal space group P4(1)2(1)2, with unit-cell parameters a = b = 42.231, c = 93.655 A, and that diffracts to 1.45 A resolution. For both WT Spc-SH3 and the GDS mutant, light-scattering experiments showed that a dimer was formed in solution within a few minutes of the addition of 2 M ammonium sulfate at pH 6.5 and allowed the proposal of a mechanism for the nucleation and crystal growth of Spc-SH3 in which the Pro20 residue plays a key role in the rate of crystal growth.

The effect of a proline residue on the rate of growth and the space group of alpha-spectrin SH3-domain crystals.,Camara-Artigas A, Andujar-Sanchez M, Ortiz-Salmeron E, Cuadri C, Casares S Acta Crystallogr D Biol Crystallogr. 2009 Dec;65(Pt 12):1247-52. Epub 2009, Nov 17. PMID:19966410<ref>PMID:19966410</ref>

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

~~</div>~~

~~<div class="pdbe-citations 3m0u" style="background-color:#fffaf0;"></div>~~

==See Also==

*[[Spectrin|Spectrin]]

*[[Spectrin 3D structures|Spectrin 3D structures]]

~~== References ==~~

~~<references/>~~

__TOC__

</StructureSection>

[[Category: ~~Chick~~]]

[[Category: Gallus gallus]]

[[Category: Large Structures]]

[[Category: Camara-Artigas, A]]

[[Category: Camara-Artigas A]]

[[Category: Gavira~~, J A]]~~

[[Category: Gavira JA]]

~~[[Category: Actin capping]]~~

~~[[Category: Actin-binding]]~~

~~[[Category: Calmodulin-binding]]~~

~~[[Category: Cytoskeleton]]~~

~~[[Category: Phosphoprotein]]~~

~~[[Category: Sh3 domain]]~~

~~[[Category: Sh3-like barrel]]~~

~~[[Category: Signaling protein~~]]

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@@ Line 3: / Line 3: @@
 <StructureSection load='3m0u' size='340' side='right'caption='[[3m0u]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3m0u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M0U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M0U FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3m0u]] 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=3M0U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M0U FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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]] 1.1&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1shg|1shg]], [[3i9q|3i9q]], [[2f2w|2f2w]], [[2f2x|2f2x]], [[3m0p|3m0p]], [[3m0q|3m0q]], [[3m0r|3m0r]], [[3m0s|3m0s]], [[3m0t|3m0t]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SPTAN1, SPTA2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK])</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=3m0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m0u OCA], [https://pdbe.org/3m0u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m0u RCSB], [https://www.ebi.ac.uk/pdbsum/3m0u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m0u ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/SPTN1_CHICK SPTN1_CHICK]] Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization.
+[https://www.uniprot.org/uniprot/SPTN1_CHICK SPTN1_CHICK] Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-alpha-Spectrin SH3-domain (Spc-SH3) crystallization is characterized by very fast growth of the crystals in the presence of ammonium sulfate as a precipitant agent. The origin of this behaviour can be attributed to the presence of a proline residue that participates in a crystal contact mimicking the binding of proline-rich sequences to SH3 domains. This residue, Pro20, is located in the RT loop and is the main contact in one of the interfaces present in the orthorhombic Spc-SH3 crystal structures. In order to understand the molecular interactions that are responsible for the very fast crystal growth of the wild-type (WT) Spc-SH3 crystals, the crystal structure of a triple mutant in which the residues Ser19-Pro20-Arg21 in the RT loop have been replaced by Gly19-Asp20-Ser21 (GDS Spc-SH3 mutant) has been solved. The removal of the critical proline residue results in slower nucleation of the Spc-SH3 crystals and a different arrangement of the protein molecules in the unit cell, leading to a crystal that belongs to the tetragonal space group P4(1)2(1)2, with unit-cell parameters a = b = 42.231, c = 93.655 A, and that diffracts to 1.45 A resolution. For both WT Spc-SH3 and the GDS mutant, light-scattering experiments showed that a dimer was formed in solution within a few minutes of the addition of 2 M ammonium sulfate at pH 6.5 and allowed the proposal of a mechanism for the nucleation and crystal growth of Spc-SH3 in which the Pro20 residue plays a key role in the rate of crystal growth.
-The effect of a proline residue on the rate of growth and the space group of alpha-spectrin SH3-domain crystals.,Camara-Artigas A, Andujar-Sanchez M, Ortiz-Salmeron E, Cuadri C, Casares S Acta Crystallogr D Biol Crystallogr. 2009 Dec;65(Pt 12):1247-52. Epub 2009, Nov 17. PMID:19966410<ref>PMID:19966410</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3m0u" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Spectrin|Spectrin]]
+*[[Spectrin 3D structures|Spectrin 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Chick]]
+[[Category: Gallus gallus]]
 [[Category: Large Structures]]
-[[Category: Camara-Artigas, A]]
+[[Category: Camara-Artigas A]]
-[[Category: Gavira, J A]]
+[[Category: Gavira JA]]
-[[Category: Actin capping]]
-[[Category: Actin-binding]]
-[[Category: Calmodulin-binding]]
-[[Category: Cytoskeleton]]
-[[Category: Phosphoprotein]]
-[[Category: Sh3 domain]]
-[[Category: Sh3-like barrel]]
-[[Category: Signaling protein]]