View source for 2rmp


==RMP-pepstatin A complex==
<StructureSection load='2rmp' size='340' side='right'caption='[[2rmp]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2rmp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhizomucor_miehei Rhizomucor miehei] and [https://en.wikipedia.org/wiki/Streptomyces Streptomyces]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RMP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RMP FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=IVA:ISOVALERIC+ACID'>IVA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=STA:STATINE'>STA</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=2rmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rmp OCA], [https://pdbe.org/2rmp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rmp RCSB], [https://www.ebi.ac.uk/pdbsum/2rmp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rmp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CARP_RHIMI CARP_RHIMI] This enzyme, capable of clotting milk is frequently used for cheese production.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rm/2rmp_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2rmp ConSurf].
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== Publication Abstract from PubMed ==
Crystals of Rhizomucor miehei aspartic proteinase (RMP) complexed with pepstatin A grew in the orthorhombic space group P212121 and were isomorphous to native RMP crystals. The unit-cell dimensions are a = 41.52, b = 50.82, c = 172.71 A. There is one RMP-pepstatin A complex per asymmetric unit. The structure of the RMP-pepstatin A complex has been refined to a crystallographic R value of 19.3% and an Rfree value of 28.0% at 2.7 A resolution. A pepstatin A molecule fits into the large substrate-binding cleft between the two domains of RMP in an extended conformation up to the alanine residue at the P2' position. The dipeptide analogue statine residue at the P3'-P4' position forms an inverse gamma-turn (P3'-P1') with the statine residue at the P1-P1' position and its leucyl side chain binds back into the S1' subsite. The inhibitor interacts with the residues of the substrate-binding pocket by both hydrogen bonds and hydrophobic interactions. The hydroxyl group of the statine residue at the P1-P1' position forms hydrogen bonds with both catalytic aspartate residues (Asp38 and Asp237). This conformation mimics the expected transition state of the enzyme-substrate interaction. The binding of the inhibitor to the enzyme does not produce large distortions of the active site. No domain movement was observed compared with the native enzyme structure. However, the surface-flap region (residues 82-88) undergoes a conformational change, moving toward the inhibitor and becoming rigid owing to the formation of hydrogen bonds with the inhibitor. B-factor calculations of the two domains suggest that the C-terminal domain becomes more rigid in the complex than in the native structure.

Structure of the Rhizomucor miehei aspartic proteinase complexed with the inhibitor pepstatin A at 2.7 A resolution.,Yang J, Quail JW Acta Crystallogr D Biol Crystallogr. 1999 Mar;55(Pt 3):625-30. PMID:10089458<ref>PMID:10089458</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 2rmp" style="background-color:#fffaf0;"></div>

==See Also==
*[[Pepsin|Pepsin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rhizomucor miehei]]
[[Category: Streptomyces]]
[[Category: Quail JW]]
[[Category: Yang J]]