5es7: Difference between revisions

Line 1:

'''~~Unreleased structure~~'''

==Crystal structure of the F-A domains of the LgrA initiation module soaked with FON, AMPcPP, and valine.==

~~The entry~~ 5es7 is ~~ON HOLD until Paper Publication~~

== Structural highlights ==

<table><tr><td colspan='2'>[[5es7]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ES7 OCA]. For a guided tour on the structure components use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ES7 FirstGlance].

~~Authors~~: ~~Reimer~~, J.M., ~~Aloise~~, M.N., ~~Schmeing, T~~.M.

</td></tr><tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</td><td class="sblockDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=FON:N-{[4-({[(6R)-2-AMINO-5-FORMYL-4-OXO-1,4,5,6,7,8-HEXAHYDROPTERIDIN-6-YL]METHYL}AMINO)PHENYL]CARBONYL}-L-GLUTAMIC+ACID'>FON</scene>, <scene name='pdbligand=VAL:VALINE'>VAL</scene></td></tr>

~~Description:~~

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5es7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5es7 OCA], [http://pdbe.org/5es7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5es7 RCSB], [http://www.ebi.ac.uk/pdbsum/5es7 PDBsum]</td></tr>

[[~~Category~~: ~~Unreleased Structures~~]]

</table>

[[Category: Aloise, M.N]]

== Function ==

[[Category: Reimer, J.M]]

[[http://www.uniprot.org/uniprot/LGRA_BREPA LGRA_BREPA]] Activates valine (or leucine, but much less frequently), and then glycine and catalyzes the formation of the peptide bond in the first step of peptide synthesis. This enzyme may also play a role in N-formylation of the first amino acid residue in the synthesized dipeptide.

[[Category: Schmeing, T.M]]

__TOC__

</StructureSection>

[[Category: Aloise, M N]]

[[Category: Reimer, J M]]

[[Category: Schmeing, T M]]

[[Category: Adenylation domain]]

[[Category: Formylation domain]]

[[Category: Initiation module]]

[[Category: Ligase]]

[[Category: Nrp]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Crystal structure of the F-A domains of the LgrA initiation module soaked with FON, AMPcPP, and valine.==
+<StructureSection load='5es7' size='340' side='right' caption='[[5es7]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
-The entry 5es7 is ON HOLD  until Paper Publication
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5es7]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ES7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ES7 FirstGlance]. <br>
-Authors: Reimer, J.M., Aloise, M.N., Schmeing, T.M.
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=FON:N-{[4-({[(6R)-2-AMINO-5-FORMYL-4-OXO-1,4,5,6,7,8-HEXAHYDROPTERIDIN-6-YL]METHYL}AMINO)PHENYL]CARBONYL}-L-GLUTAMIC+ACID'>FON</scene>, <scene name='pdbligand=VAL:VALINE'>VAL</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5es5|5es5]], [[5es6|5es6]], [[5es8|5es8]], [[5es9|5es9]]</td></tr>
-Description:
+<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=5es7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5es7 OCA], [http://pdbe.org/5es7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5es7 RCSB], [http://www.ebi.ac.uk/pdbsum/5es7 PDBsum]</span></td></tr>
-[[Category: Unreleased Structures]]
+</table>
-[[Category: Aloise, M.N]]
+== Function ==
-[[Category: Reimer, J.M]]
+[[http://www.uniprot.org/uniprot/LGRA_BREPA LGRA_BREPA]] Activates valine (or leucine, but much less frequently), and then glycine and catalyzes the formation of the peptide bond in the first step of peptide synthesis. This enzyme may also play a role in N-formylation of the first amino acid residue in the synthesized dipeptide.
-[[Category: Schmeing, T.M]]
+__TOC__
+</StructureSection>
+[[Category: Aloise, M N]]
+[[Category: Reimer, J M]]
+[[Category: Schmeing, T M]]
+[[Category: Adenylation domain]]
+[[Category: Formylation domain]]
+[[Category: Initiation module]]
+[[Category: Ligase]]
+[[Category: Nrp]]