1amu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:32, 7 February 2024) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1amu.gif|left|200px]]
 
-
{{Structure
+
==PHENYLALANINE ACTIVATING DOMAIN OF GRAMICIDIN SYNTHETASE 1 IN A COMPLEX WITH AMP AND PHENYLALANINE==
-
|PDB= 1amu |SIZE=350|CAPTION= <scene name='initialview01'>1amu</scene>, resolution 1.9&Aring;
+
<StructureSection load='1amu' size='340' side='right'caption='[[1amu]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene> and <scene name='pdbligand=AMP:ADENOSINE MONOPHOSPHATE'>AMP</scene>
+
<table><tr><td colspan='2'>[[1amu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevibacillus_brevis Brevibacillus brevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AMU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AMU FirstGlance]. <br>
-
|ACTIVITY= [http://en.wikipedia.org/wiki/Phenylalanine_racemase_(ATP-hydrolyzing) Phenylalanine racemase (ATP-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.1.11 5.1.1.11]
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
-
|GENE= GRSA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1393 Brevibacillus brevis])
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1amu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1amu OCA], [https://pdbe.org/1amu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1amu RCSB], [https://www.ebi.ac.uk/pdbsum/1amu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1amu ProSAT]</span></td></tr>
-
 
+
</table>
-
'''PHENYLALANINE ACTIVATING DOMAIN OF GRAMICIDIN SYNTHETASE 1 IN A COMPLEX WITH AMP AND PHENYLALANINE'''
+
== Function ==
-
 
+
[https://www.uniprot.org/uniprot/GRSA_ANEMI GRSA_ANEMI] In the first step of peptide synthesis this enzyme activates phenylalanine and racemizes it to the D-isomer.
-
 
+
== Evolutionary Conservation ==
-
==Overview==
+
[[Image:Consurf_key_small.gif|200px|right]]
-
The non-ribosomal synthesis of the cyclic peptide antibiotic gramicidin S is accomplished by two large multifunctional enzymes, the peptide synthetases 1 and 2. The enzyme complex contains five conserved subunits of approximately 60 kDa which carry out ATP-dependent activation of specific amino acids and share extensive regions of sequence similarity with adenylating enzymes such as firefly luciferases and acyl-CoA ligases. We have determined the crystal structure of the N-terminal adenylation subunit in a complex with AMP and L-phenylalanine to 1.9 A resolution. The 556 amino acid residue fragment is folded into two domains with the active site situated at their interface. Each domain of the enzyme has a similar topology to the corresponding domain of unliganded firefly luciferase, but a remarkable relative domain rotation of 94 degrees occurs. This conformation places the absolutely conserved Lys517 in a position to form electrostatic interactions with both ligands. The AMP is bound with the phosphate moiety interacting with Lys517 and the hydroxyl groups of the ribose forming hydrogen bonds with Asp413. The phenylalanine substrate binds in a hydrophobic pocket with the carboxylate group interacting with Lys517 and the alpha-amino group with Asp235. The structure reveals the role of the invariant residues within the superfamily of adenylate-forming enzymes and indicates a conserved mechanism of nucleotide binding and substrate activation.
+
Check<jmol>
-
 
+
<jmolCheckbox>
-
==About this Structure==
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/am/1amu_consurf.spt"</scriptWhenChecked>
-
1AMU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Brevibacillus_brevis Brevibacillus brevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AMU OCA].
+
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
-
 
+
<text>to colour the structure by Evolutionary Conservation</text>
-
==Reference==
+
</jmolCheckbox>
-
Structural basis for the activation of phenylalanine in the non-ribosomal biosynthesis of gramicidin S., Conti E, Stachelhaus T, Marahiel MA, Brick P, EMBO J. 1997 Jul 16;16(14):4174-83. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9250661 9250661]
+
</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=1amu ConSurf].
 +
<div style="clear:both"></div>
 +
__TOC__
 +
</StructureSection>
[[Category: Brevibacillus brevis]]
[[Category: Brevibacillus brevis]]
-
[[Category: Phenylalanine racemase (ATP-hydrolyzing)]]
+
[[Category: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: Brick P]]
-
[[Category: Brick, P.]]
+
[[Category: Conti E]]
-
[[Category: Conti, E.]]
+
[[Category: Marahiel MA]]
-
[[Category: Marahiel, M A.]]
+
[[Category: Stachelhaus T]]
-
[[Category: Stachelhaus, T.]]
+
-
[[Category: AMP]]
+
-
[[Category: MG]]
+
-
[[Category: PHE]]
+
-
[[Category: SO4]]
+
-
[[Category: adenylate forming]]
+
-
[[Category: grsa]]
+
-
[[Category: peptide synthetase]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:59:41 2008''
+

Current revision

PHENYLALANINE ACTIVATING DOMAIN OF GRAMICIDIN SYNTHETASE 1 IN A COMPLEX WITH AMP AND PHENYLALANINE

PDB ID 1amu

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/1amu"
Personal tools