3ndp
From Proteopedia
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==Crystal structure of human AK4(L171P)== | ==Crystal structure of human AK4(L171P)== | ||
| - | <StructureSection load='3ndp' size='340' side='right' caption='[[3ndp]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='3ndp' size='340' side='right'caption='[[3ndp]], [[Resolution|resolution]] 2.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3ndp]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3ndp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NDP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NDP FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |
| - | <tr id=' | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ndp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ndp OCA], [https://pdbe.org/3ndp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ndp RCSB], [https://www.ebi.ac.uk/pdbsum/3ndp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ndp ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/KAD4_HUMAN KAD4_HUMAN] Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. May also be active with GTP (By similarity). |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nd/3ndp_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nd/3ndp_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</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=3ndp ConSurf]. | </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=3ndp ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | It is well known that motion of LID and NMP-binding (NMP(bind)) domains in adenylate kinase (AK) is important in ligand binding and catalysis. However, the nature of such domain motions is poorly characterized. One of the critical hinge regions is hinge IV, which connects the CORE and LID domains. In addition, the hinge IV contains a strictly conserved residue, L171, in the AK family. To investigate the role of hinge IV, crystal structure of human adenylate kinase 4 (AK4) L171P mutant was determined. This mutation dramatically changes the orientation of the LID domain, which could be described as a novel twisted-and-closed conformation in contrast to the open and closed conformations in other AKs. This mutant provides a new example of domain motions in AK family. | ||
| - | + | ==See Also== | |
| - | + | *[[Adenylate kinase 3D structures|Adenylate kinase 3D structures]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Gong | + | [[Category: Gong W]] |
| - | [[Category: Liu | + | [[Category: Liu R]] |
| - | [[Category: Wang | + | [[Category: Wang Y]] |
| - | [[Category: Wei | + | [[Category: Wei Z]] |
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Current revision
Crystal structure of human AK4(L171P)
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Categories: Homo sapiens | Large Structures | Gong W | Liu R | Wang Y | Wei Z
