1h7n: 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: @@
-[[Image:1h7n.jpg|left|200px]]
- {{Structure
+==SCHIFF-BASE COMPLEX OF YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE WITH LAEVULINIC ACID AT 1.6 A RESOLUTION==
-|PDB= 1h7n |SIZE=350|CAPTION= <scene name='initialview01'>1h7n</scene>, resolution 1.6&Aring;
+<StructureSection load='1h7n' size='340' side='right'caption='[[1h7n]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
-|SITE= <scene name='pdbsite=AC1:Shf+Binding+Site+For+Chain+A'>AC1</scene> and <scene name='pdbsite=AC2:Zn+Binding+Site+For+Chain+A'>AC2</scene>
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=SHF:LAEVULINIC+ACID'>SHF</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
+<table><tr><td colspan='2'>[[1h7n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H7N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H7N FirstGlance]. <br>
-|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Porphobilinogen_synthase Porphobilinogen synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.24 4.2.1.24] </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]] 1.6&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SHF:LAEVULINIC+ACID'>SHF</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1h7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h7n OCA], [https://pdbe.org/1h7n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h7n RCSB], [https://www.ebi.ac.uk/pdbsum/1h7n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h7n ProSAT]</span></td></tr>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h7n OCA], [http://www.ebi.ac.uk/pdbsum/1h7n PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h7n RCSB]</span>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/HEM2_YEAST HEM2_YEAST] Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.
+== 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/h7/1h7n_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=1h7n ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The structures of 5-aminolaevulinic acid dehydratase (ALAD) complexed with substrate (5-aminolaevulinic acid) and three inhibitors: laevulinic acid, succinylacetone and 4-keto-5-aminolaevulinic acid, have been solved at high resolution. The ligands all bind by forming a covalent link with Lys263 at the active site. The structures define the interactions made by one of the two substrate moieties that bind to the enzyme during catalysis. All of the inhibitors induce a significant ordering of the flap covering the active site. Succinylacetone appears to be unique by inducing a number of conformational changes in loops covering the active site, which may be important for understanding the co-operative properties of ALAD enzymes. Succinylacetone is produced in large amounts by patients suffering from the hereditary disease type I tyrosinaemia and its potent inhibition of ALAD also has implications for the pathology of this disease. The most intriguing result is that obtained with 4-keto-5-amino-hexanoic acid, which seems to form a stable carbinolamine intermediate with Lys263. It appears that we have defined the structure of an intermediate of Schiff base formation that the substrate forms upon binding to the P-site of the enzyme.
-'''SCHIFF-BASE COMPLEX OF YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE WITH LAEVULINIC ACID AT 1.6 A RESOLUTION'''
+The x-ray structure of yeast 5-aminolaevulinic acid dehydratase complexed with substrate and three inhibitors.,Erskine PT, Newbold R, Brindley AA, Wood SP, Shoolingin-Jordan PM, Warren MJ, Cooper JB J Mol Biol. 2001 Sep 7;312(1):133-41. PMID:11545591<ref>PMID:11545591</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1h7n" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-The structures of 5-aminolaevulinic acid dehydratase (ALAD) complexed with substrate (5-aminolaevulinic acid) and three inhibitors: laevulinic acid, succinylacetone and 4-keto-5-aminolaevulinic acid, have been solved at high resolution. The ligands all bind by forming a covalent link with Lys263 at the active site. The structures define the interactions made by one of the two substrate moieties that bind to the enzyme during catalysis. All of the inhibitors induce a significant ordering of the flap covering the active site. Succinylacetone appears to be unique by inducing a number of conformational changes in loops covering the active site, which may be important for understanding the co-operative properties of ALAD enzymes. Succinylacetone is produced in large amounts by patients suffering from the hereditary disease type I tyrosinaemia and its potent inhibition of ALAD also has implications for the pathology of this disease. The most intriguing result is that obtained with 4-keto-5-amino-hexanoic acid, which seems to form a stable carbinolamine intermediate with Lys263. It appears that we have defined the structure of an intermediate of Schiff base formation that the substrate forms upon binding to the P-site of the enzyme.
+*[[Porphobilinogen synthase|Porphobilinogen synthase]]
+== References ==
-==About this Structure==
+<references/>
-H7N is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H7N OCA].
+__TOC__
+</StructureSection>
-==Reference==
+[[Category: Large Structures]]
-The x-ray structure of yeast 5-aminolaevulinic acid dehydratase complexed with substrate and three inhibitors., Erskine PT, Newbold R, Brindley AA, Wood SP, Shoolingin-Jordan PM, Warren MJ, Cooper JB, J Mol Biol. 2001 Sep 7;312(1):133-41. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11545591 11545591]
-[[Category: Porphobilinogen synthase]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Single protein]]
+[[Category: Brindley AA]]
-[[Category: Brindley, A A.]]
+[[Category: Cooper JB]]
-[[Category: Cooper, J B.]]
+[[Category: Erskine PT]]
-[[Category: Erskine, P T.]]
+[[Category: Newbold R]]
-[[Category: Newbold, R.]]
+[[Category: Shoolingin-Jordan PM]]
-[[Category: Shoolingin-Jordan, P M.]]
+[[Category: Warren MJ]]
-[[Category: Warren, M J.]]
+[[Category: Wood SP]]
-[[Category: Wood, S P.]]
-[[Category: aldolase]]
-[[Category: dehydratase]]
-[[Category: lyase]]
-[[Category: tetrapyrrole synthesis]]
-[[Category: tim barrel]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:59:35 2008''