1xsa: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:1xsa.png|left|200px]]
-<!--
+==Structure of the nudix enzyme AP4A hydrolase from homo sapiens (E63A mutant)==
-The line below this paragraph, containing "STRUCTURE_1xsa", creates the "Structure Box" on the page.
+<StructureSection load='1xsa' size='340' side='right'caption='[[1xsa]]' 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'>[[1xsa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XSA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XSA 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">Solution NMR</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=1xsa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xsa OCA], [https://pdbe.org/1xsa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xsa RCSB], [https://www.ebi.ac.uk/pdbsum/1xsa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xsa ProSAT]</span></td></tr>
-{{STRUCTURE_1xsa|  PDB=1xsa  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/AP4A_HUMAN AP4A_HUMAN] Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Plays a major role in maintaining homeostasis.
+== 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/xs/1xsa_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=1xsa ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Asymmetric diadenosine 5',5'''-P(1),P(4)-tetraphosphate (Ap(4)A) hydrolases play a major role in maintaining homeostasis by cleaving the metabolite diadenosine tetraphosphate (Ap(4)A) back into ATP and AMP. The NMR solution structures of the 17-kDa human asymmetric Ap(4)A hydrolase have been solved in both the presence and absence of the product ATP. The adenine moiety of the nucleotide predominantly binds in a ring stacking arrangement equivalent to that observed in the x-ray structure of the homologue from Caenorhabditis elegans. The binding site is, however, markedly divergent to that observed in the plant/pathogenic bacteria class of enzymes, opening avenues for the exploration of specific therapeutics. Binding of ATP induces substantial conformational and dynamic changes that were not observed in the C. elegans structure. In contrast to the C. elegans homologue, important side chains that play a major role in substrate binding do not have to reorient to accommodate the ligand. This may have important implications in the mechanism of substrate recognition in this class of enzymes.
-===Structure of the nudix enzyme AP4A hydrolase from homo sapiens (E63A mutant)===
+Structure and substrate-binding mechanism of human Ap4A hydrolase.,Swarbrick JD, Buyya S, Gunawardana D, Gayler KR, McLennan AG, Gooley PR J Biol Chem. 2005 Mar 4;280(9):8471-81. Epub 2004 Dec 13. PMID:15596429<ref>PMID:15596429</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_15596429}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1xsa" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 15596429 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_15596429}}
+__TOC__
+</StructureSection>
-==About this Structure==
-XSA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XSA OCA].
-==Reference==
-Structure and substrate-binding mechanism of human Ap4A hydrolase., Swarbrick JD, Buyya S, Gunawardana D, Gayler KR, McLennan AG, Gooley PR, J Biol Chem. 2005 Mar 4;280(9):8471-81. Epub 2004 Dec 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15596429 15596429]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Buyya, S.]]
+[[Category: Buyya S]]
-[[Category: Gayler, K R.]]
+[[Category: Gayler KR]]
-[[Category: Gooley, P R.]]
+[[Category: Gooley PR]]
-[[Category: Gunawardana, D.]]
+[[Category: Gunawardana D]]
-[[Category: McLennan, A G.]]
+[[Category: McLennan AG]]
-[[Category: Swarbrick, J D.]]
+[[Category: Swarbrick JD]]
-[[Category: Alpha-beta]]
-[[Category: Human ap4a hydrolase]]
-[[Category: Nmr]]
-[[Category: Nudix enzyme]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:53:57 2008''