2a3l

<table><tr><td colspan='2'>[[2a3l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A3L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A3L FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CF5:COFORMYCIN+5-PHOSPHATE'>CF5</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At2g38280 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>

[[https://www.uniprot.org/uniprot/AMPD_ARATH AMPD_ARATH]] AMP deaminase plays a critical role in energy metabolism. Essential for the transition from zygote to embryo.<ref>PMID:15918887</ref>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Embryonic factor 1 (FAC1) is one of the earliest expressed plant genes and encodes an AMP deaminase (AMPD), which is also an identified herbicide target. This report identifies an N-terminal transmembrane domain in Arabidopsis FAC1, explores subcellular fractionation, and presents a 3.3-A globular catalytic domain x-ray crystal structure with a bound herbicide-based transition state inhibitor that provides the first glimpse of a complete AMPD active site. FAC1 contains an (alpha/beta)(8)-barrel characterized by loops in place of strands 5 and 6 that places it in a small subset of the amidohydrolase superfamily with imperfect folds. Unlike tetrameric animal orthologs, FAC1 is a dimer and each subunit contains an exposed Walker A motif that may be involved in the dramatic combined K(m) (25-80-fold lower) and V(max) (5-6-fold higher) activation by ATP. Normal mode analysis predicts a hinge motion that flattens basic surfaces on each monomer that flank the dimer interface, which suggests a reversible association between the FAC1 globular catalytic domain and intracellular membranes, with N-terminal transmembrane and disordered linker regions serving as the anchor and attachment to the globular catalytic domain, respectively.

Membrane association, mechanism of action, and structure of Arabidopsis embryonic factor 1 (FAC1).,Han BW, Bingman CA, Mahnke DK, Bannen RM, Bednarek SY, Sabina RL, Phillips GN Jr J Biol Chem. 2006 May 26;281(21):14939-47. Epub 2006 Mar 16. PMID:16543243<ref>PMID:16543243</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 2a3l" style="background-color:#fffaf0;"></div>

[[Category: Arath]]

[[Category: Allard, S T.M]]

[[Category: Bingman, C A]]

[[Category: Bitto, E]]

[[Category: Structural genomic]]

[[Category: Han, B W]]

[[Category: Phillips, G N]]

[[Category: Wesenberg, G E]]

[[Category: PSI, Protein structure initiative]]