4lj3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 2: Line 2:
<StructureSection load='4lj3' size='340' side='right' caption='[[4lj3]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='4lj3' size='340' side='right' caption='[[4lj3]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4lj3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LJ3 OCA]. <br>
+
<table><tr><td colspan='2'>[[4lj3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LJ3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LJ3 FirstGlance]. <br>
-
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C2E:9,9-[(2R,3R,3AS,5S,7AR,9R,10R,10AS,12S,14AR)-3,5,10,12-TETRAHYDROXY-5,12-DIOXIDOOCTAHYDRO-2H,7H-DIFURO[3,2-D 3,2-J][1,3,7,9,2,8]TETRAOXADIPHOSPHACYCLODODECINE-2,9-DIYL]BIS(2-AMINO-1,9-DIHYDRO-6H-PURIN-6-ONE)'>C2E</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HB0:TRANS-4-(HYDROXYMETHYL)CYCLOHEXANOL'>HB0</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene><br>
+
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C2E:9,9-[(2R,3R,3AS,5S,7AR,9R,10R,10AS,12S,14AR)-3,5,10,12-TETRAHYDROXY-5,12-DIOXIDOOCTAHYDRO-2H,7H-DIFURO[3,2-D 3,2-J][1,3,7,9,2,8]TETRAOXADIPHOSPHACYCLODODECINE-2,9-DIYL]BIS(2-AMINO-1,9-DIHYDRO-6H-PURIN-6-ONE)'>C2E</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HB0:TRANS-4-(HYDROXYMETHYL)CYCLOHEXANOL'>HB0</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr>
-
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kie|4kie]], [[4lyk|4lyk]]</td></tr>
+
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kie|4kie]], [[4lyk|4lyk]]</td></tr>
-
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yahA, b0315, JW0307 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
+
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yahA, b0315, JW0307 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
-
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4lj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lj3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lj3 RCSB], [http://www.ebi.ac.uk/pdbsum/4lj3 PDBsum]</span></td></tr>
-
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4lj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lj3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lj3 RCSB], [http://www.ebi.ac.uk/pdbsum/4lj3 PDBsum]</span></td></tr>
+
</table>
-
<table>
+
== Function ==
 +
[[http://www.uniprot.org/uniprot/YAHA_ECOLI YAHA_ECOLI]] Hydrolyzes c-di-GMP (cyclic bis(3'-5') dimeric GMP) to 5'-pGpG, known as PDE-A activity. PDE-B activity, that is hydrolysis of 5'-pGpG to GMP, proceeds only very slowly.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 15: Line 16:
Inherent regulation of EAL domain-catalyzed hydrolysis of second messenger c-di-GMP.,Sundriyal A, Massa C, Samoray D, Zehender F, Sharpe T, Jenal U, Schirmer T J Biol Chem. 2014 Jan 22. PMID:24451384<ref>PMID:24451384</ref>
Inherent regulation of EAL domain-catalyzed hydrolysis of second messenger c-di-GMP.,Sundriyal A, Massa C, Samoray D, Zehender F, Sharpe T, Jenal U, Schirmer T J Biol Chem. 2014 Jan 22. PMID:24451384<ref>PMID:24451384</ref>
-
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
 +
 +
==See Also==
 +
*[[Phosphodiesterase|Phosphodiesterase]]
== References ==
== References ==
<references/>
<references/>
Line 22: Line 26:
</StructureSection>
</StructureSection>
[[Category: Ecoli]]
[[Category: Ecoli]]
-
[[Category: Schirmer, T.]]
+
[[Category: Schirmer, T]]
-
[[Category: Sundriyal, A.]]
+
[[Category: Sundriyal, A]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Pgpg]]
[[Category: Pgpg]]
[[Category: Phosphodiesterase]]
[[Category: Phosphodiesterase]]
[[Category: Tim-barrel]]
[[Category: Tim-barrel]]

Revision as of 14:27, 25 December 2014

Crystal structure of the EAL domain of c-di-GMP specific phosphodiesterase YahA in complex with substrate c-di-GMP and Ca++

4lj3, resolution 1.70Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4lj3"
Personal tools