1e5o

<table><tr><td colspan='2'>[[1e5o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Endothia_parasitica Endothia parasitica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E5O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E5O FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3AI:N-[(2S)-2-AMINO-3-PHENYLPROPYL]-D-METHIONYL-L-ALANYL-L-ISOLEUCINE'>3AI</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4ape|4ape]], [[2er0|2er0]], [[4er1|4er1]], [[5er1|5er1]], [[4er2|4er2]], [[5er2|5er2]], [[3er3|3er3]], [[4er4|4er4]], [[3er5|3er5]], [[2er6|2er6]], [[2er7|2er7]], [[1er8|1er8]], [[2er9|2er9]], [[1eed|1eed]], [[1ent|1ent]], [[1epl|1epl]], [[1epm|1epm]], [[1epn|1epn]], [[1epo|1epo]], [[1epp|1epp]], [[1epq|1epq]], [[1epr|1epr]]</div></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Mucorpepsin Mucorpepsin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.23 3.4.23.23] </span></td></tr>

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== Publication Abstract from PubMed ==

BACKGROUND: Sequence alignment suggests that xylanases evolved from two ancestral proteins and therefore can be grouped into two families, designated F and G. Family F enzymes show no sequence similarity with any known structure and their architecture is unknown. Studies of an inactive enzyme-substrate complex will help to elucidate the structural basis of binding and catalysis in the family F xylanases. RESULTS: We have therefore determined the crystal structure of the catalytic domain of a family F enzyme, Pseudomonas fluorescens subsp. cellulosa xylanase A, at 2.5 A resolution and a crystallographic R-factor of 0.20. The structure was solved using an engineered catalytic core in which the nucleophilic glutamate was replaced by a cysteine. As expected, this yielded both high-quality mercurial derivatives and an inactive enzyme which enabled the preparation of the inactive enzyme-substrate complex in the crystal. We show that family F xylanases are eight-fold alpha/beta-barrels (TIM barrels) with two active-site glutamates, one of which is the nucleophile and the other the acid-base. Xylopentaose binds to five subsites A-E with the cleaved bond between subsites D and E. Ca2+ binding, remote from the active-site glutamates, stabilizes the structure and may be involved in the binding of extended substrates. CONCLUSIONS: The architecture of P. fluorescens subsp. cellulosa has been determined crystallographically to be a commonly occurring enzyme fold, the eight-fold alpha/beta-barrel. Xylopentaose binds across the carboxy-terminal end of the alpha/beta-barrel in an active-site cleft which contains the two catalytic glutamates.

Structure of the catalytic core of the family F xylanase from Pseudomonas fluorescens and identification of the xylopentaose-binding sites.,Harris GW, Jenkins JA, Connerton I, Cummings N, Lo Leggio L, Scott M, Hazlewood GP, Laurie JI, Gilbert HJ, Pickersgill RW Structure. 1994 Nov 15;2(11):1107-16. PMID:7881909<ref>PMID:7881909</ref>

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

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<div class="pdbe-citations 1e5o" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Endothia parasitica]]

[[Category: Bailey, D]]

[[Category: Cooper, J B]]

[[Category: Read, J A]]

[[Category: Toldo, L]]

[[Category: Hydrolase-hydrolase inhibitor complex]]