4cms

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Current revision

X-RAY ANALYSES OF ASPARTIC PROTEINASES IV. STRUCTURE AND REFINEMENT AT 2.2 ANGSTROMS RESOLUTION OF BOVINE CHYMOSIN

Structural highlights

4cms is a 1 chain structure with sequence from Bos taurus. The December 2000 RCSB PDB Molecule of the Month feature on Pepsin by David S. Goodsell is 10.2210/rcsb_pdb/mom_2000_12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.2Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CHYM_BOVIN Chymosin is synthesized in the mucosa of the abomasum (fourth stomach) of young (unweaned) ruminants. The enzyme hydrolyzes casein to paracasein.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The structure of calf chymosin (EC 3.4.23.3), the aspartic proteinase from the gastric mucosa, was solved using the technique of molecular replacement. We describe the use of different search models based on distantly related fungal aspartic proteinases and investigate the effect of using only structurally conserved regions. The structure has been refined to a crystallographic R-factor of 17% at 2.2 A resolution with an estimated co-ordinate error of 0.21 A. In all, 136 water molecules have been located of which eight are internal. The structure of chymosin resembles that of pepsin and other aspartic proteinases. However, there is a considerable rearrangement of the active-site "flap" and, in particular, Tyr75 (pepsin numbering), which forms part of the specificity pockets S1 and S1'. This is probably a consequence of crystal packing. Electrostatic interactions on the edge of the substrate binding cleft appear to account for the restricted proteolysis of the natural substrate kappa-casein by chymosin. The local environment of invariant residues is examined, showing that structural constraints and side-chain hydrogen bonding can play an important role in the conservation of particular amino acids.

X-ray analyses of aspartic proteinases. IV. Structure and refinement at 2.2 A resolution of bovine chymosin.,Newman M, Safro M, Frazao C, Khan G, Zdanov A, Tickle IJ, Blundell TL, Andreeva N J Mol Biol. 1991 Oct 20;221(4):1295-309. PMID:1942052^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Newman M, Safro M, Frazao C, Khan G, Zdanov A, Tickle IJ, Blundell TL, Andreeva N. X-ray analyses of aspartic proteinases. IV. Structure and refinement at 2.2 A resolution of bovine chymosin. J Mol Biol. 1991 Oct 20;221(4):1295-309. PMID:1942052

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4cms"

@@ Line 3: / Line 3: @@
 <StructureSection load='4cms' size='340' side='right'caption='[[4cms]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4cms]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. The December 2000 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Pepsin''  by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2000_12 10.2210/rcsb_pdb/mom_2000_12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CMS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CMS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4cms]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. The December 2000 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Pepsin''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2000_12 10.2210/rcsb_pdb/mom_2000_12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CMS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CMS FirstGlance]. <br>
-</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chymosin Chymosin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.4 3.4.23.4] </span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
-<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=4cms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cms OCA], [http://pdbe.org/4cms PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cms RCSB], [http://www.ebi.ac.uk/pdbsum/4cms PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cms ProSAT]</span></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=4cms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cms OCA], [https://pdbe.org/4cms PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cms RCSB], [https://www.ebi.ac.uk/pdbsum/4cms PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cms ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CHYM_BOVIN CHYM_BOVIN]] Chymosin is synthesized in the mucosa of the abomasum (fourth stomach) of young (unweaned) ruminants. The enzyme hydrolyzes casein to paracasein.
+[https://www.uniprot.org/uniprot/CHYM_BOVIN CHYM_BOVIN] Chymosin is synthesized in the mucosa of the abomasum (fourth stomach) of young (unweaned) ruminants. The enzyme hydrolyzes casein to paracasein.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 14: / Line 14: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cm/4cms_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 32: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Bovin]]
+[[Category: Bos taurus]]
-[[Category: Chymosin]]
 [[Category: Large Structures]]
 [[Category: Pepsin]]
 [[Category: RCSB PDB Molecule of the Month]]
-[[Category: Andreeva, N]]
+[[Category: Andreeva N]]
-[[Category: Blundell, T L]]
+[[Category: Blundell TL]]
-[[Category: Frazao, C]]
+[[Category: Frazao C]]
-[[Category: Khan, G]]
+[[Category: Khan G]]
-[[Category: Newman, M]]
+[[Category: Newman M]]
-[[Category: Safro, M]]
+[[Category: Safro M]]
-[[Category: Tickle, I J]]
+[[Category: Tickle IJ]]
-[[Category: Zdanov, A]]
+[[Category: Zdanov A]]

4cms

From Proteopedia

Current revision

X-RAY ANALYSES OF ASPARTIC PROTEINASES IV. STRUCTURE AND REFINEMENT AT 2.2 ANGSTROMS RESOLUTION OF BOVINE CHYMOSIN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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